UniProtKB - P56817 (BACE1_HUMAN)
Beta-secretase 1
BACE1
Functioni
Catalytic activityi
- Broad endopeptidase specificity. Cleaves Glu-Val-Asn-Leu-|-Asp-Ala-Glu-Phe in the Swedish variant of Alzheimer's amyloid precursor protein.1 Publication EC:3.4.23.46
Activity regulationi
Kineticsi
- KM=15.2 mM for APP cleaved by PSEN1 (at pH4)1 Publication
- KM=1 mM for APP Swedish variant (at pH4)1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 93 | PROSITE-ProRule annotation | 1 | |
Active sitei | 289 | PROSITE-ProRule annotation | 1 |
GO - Molecular functioni
- amyloid-beta binding Source: Alzheimers_University_of_Toronto
- aspartic-type endopeptidase activity Source: UniProtKB
- beta-aspartyl-peptidase activity Source: Reactome
- endopeptidase activity Source: UniProtKB
- enzyme binding Source: UniProtKB
- peptidase activity Source: CACAO
GO - Biological processi
- amyloid-beta metabolic process Source: UniProtKB
- amyloid precursor protein catabolic process Source: ARUK-UCL
- cellular protein metabolic process Source: Reactome
- cellular response to amyloid-beta Source: Ensembl
- cellular response to copper ion Source: Ensembl
- cellular response to manganese ion Source: Ensembl
- detection of mechanical stimulus involved in sensory perception of pain Source: Ensembl
- membrane protein ectodomain proteolysis Source: UniProtKB
- positive regulation of neuron apoptotic process Source: ARUK-UCL
- prepulse inhibition Source: Ensembl
- protein catabolic process Source: GO_Central
- proteolysis Source: UniProtKB
- regulation of synaptic vesicle exocytosis Source: Ensembl
- response to lead ion Source: Ensembl
- response to radiation Source: Ensembl
Keywordsi
Molecular function | Aspartyl protease, Hydrolase, Protease |
Enzyme and pathway databases
BioCyci | MetaCyc:ENSG00000160610-MONOMER |
BRENDAi | 3.4.23.46 2681 |
Reactomei | R-HSA-977225 Amyloid fiber formation |
SABIO-RKi | P56817 |
SIGNORi | P56817 |
Protein family/group databases
MEROPSi | A01.004 |
TCDBi | 8.A.32.1.1 the Beta-amyloid cleaving enzyme (bace1) family |
Names & Taxonomyi
Protein namesi | Recommended name: Beta-secretase 1Curated (EC:3.4.23.461 Publication)Alternative name(s): Aspartyl protease 21 Publication Short name: ASP21 Publication Short name: Asp 21 Publication Beta-site amyloid precursor protein cleaving enzyme 1 Short name: Beta-site APP cleaving enzyme 1 Memapsin-22 Publications Membrane-associated aspartic protease 2 |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:933 BACE1 |
MIMi | 604252 gene |
neXtProti | NX_P56817 |
Subcellular locationi
Endoplasmic reticulum
- Endoplasmic reticulum 2 Publications
Plasma membrane
- Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication
Golgi apparatus
- trans-Golgi network 6 Publications
Endosome
- Endosome 2 Publications
- Late endosome 4 Publications
- Early endosome 5 Publications
- Recycling endosome 3 Publications
Lysosome
- Lysosome 4 Publications
Other locations
- Cell surface 4 Publications
- Cytoplasmic vesicle membrane 2 Publications; Single-pass type I membrane protein 1 Publication
- Membrane raft By similarity
- axon By similarity
- dendrite By similarity
Note: Predominantly localized to the later Golgi/trans-Golgi network (TGN) and minimally detectable in the early Golgi compartments. A small portion is also found in the endoplasmic reticulum, endosomes and on the cell surface (PubMed:17425515, PubMed:11466313). Colocalization with APP in early endosomes is due to addition of bisecting N-acetylglucosamine wich blocks targeting to late endosomes and lysosomes (By similarity). Retrogradly transported from endosomal compartments to the trans-Golgi network in a phosphorylation- and GGA1- dependent manner (PubMed:15886016).By similarity3 Publications
Endoplasmic reticulum
- endoplasmic reticulum lumen Source: Reactome
Endosome
- early endosome Source: UniProtKB
- endosome Source: UniProtKB
- endosome membrane Source: Reactome
- late endosome Source: UniProtKB
- multivesicular body Source: UniProtKB
- recycling endosome Source: UniProtKB
Golgi apparatus
- Golgi apparatus Source: UniProtKB
- Golgi-associated vesicle lumen Source: Reactome
- trans-Golgi network Source: UniProtKB
Lysosome
- lysosome Source: UniProtKB
Plasma Membrane
- integral component of plasma membrane Source: UniProtKB
- plasma membrane Source: UniProtKB
Other locations
- axon Source: UniProtKB-SubCell
- cell surface Source: UniProtKB
- cytoplasmic vesicle membrane Source: UniProtKB-SubCell
- dendrite Source: UniProtKB-SubCell
- hippocampal mossy fiber to CA3 synapse Source: Ensembl
- integral component of membrane Source: UniProtKB
- membrane Source: GO_Central
- membrane raft Source: UniProtKB-SubCell
- neuronal cell body Source: Ensembl
- synaptic vesicle Source: Ensembl
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 22 – 457 | ExtracellularSequence analysisAdd BLAST | 436 | |
Transmembranei | 458 – 478 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 479 – 501 | CytoplasmicSequence analysisAdd BLAST | 23 |
Keywords - Cellular componenti
Cell membrane, Cell projection, Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Golgi apparatus, Lysosome, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 93 | D → N: Decreases beta-cleaved soluble APP production. 1 Publication | 1 | |
Mutagenesisi | 284 | D → N: Almost abolishes beta-cleaved soluble APP production. 1 Publication | 1 | |
Mutagenesisi | 498 | S → A: No effect on endocytosis from the cell surface. Increases recycling from endosomes to the cell surface. 2 Publications | 1 | |
Mutagenesisi | 498 | S → D: No effect on endocytosis form the cell surface. Decreases recycling from endosomes to the cell surface. 1 Publication | 1 | |
Mutagenesisi | 499 – 500 | LL → AA: Impairs endocytosis and produces a delayed retrograde transport to the trans-Golgi network and delivery to the lysosmes, decreasinf its degradation. Disrupts location to late endosomes and lysosomes. Locates mainly at the cell surface. No effect on degradation regulated by GGA3. Effects on protein stability and defective internalization increases; when associated with R-501. 4 Publications | 2 | |
Mutagenesisi | 501 | K → R: Inhibits ubiquitination. No effect on endocytosis rate. Induced protein stability and acculmulation in early and late endosomes, lysosomes and cell membrane. Effects on protein stability and defective internalization increases; when associated with A-499-500-A. 3 Publications | 1 |
Organism-specific databases
DisGeNETi | 23621 |
OpenTargetsi | ENSG00000186318 |
PharmGKBi | PA25232 |
Miscellaneous databases
Pharosi | P56817 |
Chemistry databases
ChEMBLi | CHEMBL4822 |
DrugBanki | DB07573 (2S)-1-(2,5-dimethylphenoxy)-3-morpholin-4-ylpropan-2-ol DB07736 (2S)-4-(4-fluorobenzyl)-N-(2-sulfanylethyl)piperazine-2-carboxamide DB07737 (2S)-4-(4-fluorobenzyl)-N-(3-sulfanylpropyl)piperazine-2-carboxamide DB07519 (6R)-2-amino-6-[2-(3'-methoxybiphenyl-3-yl)ethyl]-3,6-dimethyl-5,6-dihydropyrimidin-4(3H)-one DB07874 (6S)-2-amino-6-(3'-methoxybiphenyl-3-yl)-3,6-dimethyl-5,6-dihydropyrimidin-4(3H)-one DB07535 2-amino-6-[2-(1H-indol-6-yl)ethyl]pyrimidin-4(3H)-one DB08749 3-(2-AMINO-6-BENZOYLQUINAZOLIN-3(4H)-YL)-N-CYCLOHEXYL-N-METHYLPROPANAMIDE DB07345 4-(2-aminoethyl)-2-cyclohexylphenol DB07346 4-(2-aminoethyl)-2-ethylphenol DB07110 4-(4-FLUOROBENZYL)PIPERIDINE DB07415 4-[(1S)-1-(3-fluoro-4-methoxyphenyl)-2-(2-methoxy-5-nitrophenyl)ethyl]-1H-imidazol-2-amine DB07206 6-[2-(1H-INDOL-6-YL)ETHYL]PYRIDIN-2-AMINE DB07245 6-[2-(3'-METHOXYBIPHENYL-3-YL)ETHYL]PYRIDIN-2-AMINE DB06073 CTS-21166 DB02378 MMI-175 DB07734 N-(1-benzylpiperidin-4-yl)-4-sulfanylbutanamide DB07019 N-[(5R,14R)-5-AMINO-5,14-DIMETHYL-4-OXO-3-OXA-18-AZATRICYCLO[15.3.1.1~7,11~]DOCOSA-1(21),7(22),8,10,17,19-HEXAEN-19-YL]-N-METHYLMETHANESULFONAMIDE DB07735 N-[1-(2,6-dimethoxybenzyl)piperidin-4-yl]-4-sulfanylbutanamide DB07738 N-[1-(5-bromo-2,3-dimethoxybenzyl)piperidin-4-yl]-4-sulfanylbutanamide DB06930 N-[amino(imino)methyl]-2-(2,5-diphenyl-1H-pyrrol-1-yl)acetamide DB07089 N-[amino(imino)methyl]-2-[2-(2-chlorophenyl)-4-(4-propoxyphenyl)-3-thienyl]acetamide DB07175 N-{2-methyl-5-[(6-phenylpyrimidin-4-yl)amino]phenyl}methanesulfonamide DB07284 N~3~-(3-PYRIDIN-3-YLBENZYL)PYRIDINE-2,3-DIAMINE DB07993 N~3~-[3-(1H-INDOL-6-YL)BENZYL]PYRIDINE-2,3-DIAMINE DB07303 N~3~-[3-(5-METHOXYPYRIDIN-3-YL)BENZYL]PYRIDINE-2,3-DIAMINE DB07994 N~3~-[5-(1H-INDOL-6-YL)-2-(PYRIDIN-2-YLMETHOXY)BENZYL]PYRIDINE-2,3-DIAMINE DB07281 N~3~-BENZYLPYRIDINE-2,3-DIAMINE DB12285 Verubecestat |
DrugCentrali | P56817 |
GuidetoPHARMACOLOGYi | 2330 |
Polymorphism and mutation databases
BioMutai | BACE1 |
DMDMi | 296434407 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 21 | Sequence analysisAdd BLAST | 21 | |
PropeptideiPRO_0000025939 | 22 – 45 | 1 PublicationAdd BLAST | 24 | |
ChainiPRO_0000025940 | 46 – 501 | Beta-secretase 1Add BLAST | 456 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 126 | N6-acetyllysine2 Publications | 1 | |
Glycosylationi | 153 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 172 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 216 ↔ 420 | 1 Publication | ||
Glycosylationi | 223 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 275 | N6-acetyllysine2 Publications | 1 | |
Disulfide bondi | 278 ↔ 443 | 1 Publication | ||
Modified residuei | 279 | N6-acetyllysine2 Publications | 1 | |
Modified residuei | 285 | N6-acetyllysine2 Publications | 1 | |
Modified residuei | 299 | N6-acetyllysine2 Publications | 1 | |
Modified residuei | 300 | N6-acetyllysine2 Publications | 1 | |
Modified residuei | 307 | N6-acetyllysine2 Publications | 1 | |
Disulfide bondi | 330 ↔ 380 | 1 Publication | ||
Glycosylationi | 354 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Lipidationi | 474 | S-palmitoyl cysteineBy similarity | 1 | |
Lipidationi | 478 | S-palmitoyl cysteineBy similarity | 1 | |
Lipidationi | 482 | S-palmitoyl cysteineBy similarity | 1 | |
Lipidationi | 485 | S-palmitoyl cysteineBy similarity | 1 | |
Modified residuei | 498 | Phosphoserine1 Publication | 1 | |
Cross-linki | 501 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications |
Post-translational modificationi
Keywords - PTMi
Acetylation, Disulfide bond, Glycoprotein, Isopeptide bond, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation, ZymogenProteomic databases
jPOSTi | P56817 |
MassIVEi | P56817 |
PaxDbi | P56817 |
PeptideAtlasi | P56817 |
PRIDEi | P56817 |
ProteomicsDBi | 19820 43307 56947 [P56817-1] 56948 [P56817-2] 56949 [P56817-3] 56950 [P56817-4] |
PTM databases
GlyConnecti | 71 72 |
iPTMneti | P56817 |
PhosphoSitePlusi | P56817 |
SwissPalmi | P56817 |
UniCarbKBi | P56817 |
Miscellaneous databases
PMAP-CutDBi | P56817 |
Expressioni
Tissue specificityi
Inductioni
Gene expression databases
Bgeei | ENSG00000186318 Expressed in 223 organ(s), highest expression level in C1 segment of cervical spinal cord |
ExpressionAtlasi | P56817 baseline and differential |
Genevisiblei | P56817 HS |
Organism-specific databases
HPAi | CAB016358 |
Interactioni
Subunit structurei
Monomer.
Interacts (via DXXLL motif) with GGA1, GGA2 and GGA3 (via their VHS domain); the interaction highly increases when BACE1 is phosphorylated at Ser-498 (PubMed:14567678, PubMed:15886016).
Interacts with RTN3 and RTN4 (PubMed:15286784, PubMed:16965550, PubMed:16979658).
Interacts with SNX6 (PubMed:20354142).
Interacts with PCSK9 (PubMed:18660751).
Interacts with NAT8 and NAT8B (PubMed:19011241).
Interacts with BIN1 (PubMed:27179792).
Interacts (via extracellular domain) with ADAM10 (via extracellular domain) (By similarity).
Interacts with SORL1; this interaction may affect binding with APP and hence reduce APP cleavage (PubMed:16407538).
By similarity10 PublicationsBinary interactionsi
GO - Molecular functioni
- enzyme binding Source: UniProtKB
Protein-protein interaction databases
BioGridi | 117154, 21 interactors |
CORUMi | P56817 |
DIPi | DIP-41388N |
IntActi | P56817, 40 interactors |
MINTi | P56817 |
STRINGi | 9606.ENSP00000318585 |
Chemistry databases
BindingDBi | P56817 |
Structurei
Secondary structure
3D structure databases
SMRi | P56817 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P56817 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 75 – 416 | Peptidase A1PROSITE-ProRule annotationAdd BLAST | 342 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 479 – 501 | Interaction with RTN3Add BLAST | 23 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 496 – 500 | DXXLL1 Publication | 5 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Signal, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG1339 Eukaryota ENOG410XNV7 LUCA |
GeneTreei | ENSGT00940000157786 |
InParanoidi | P56817 |
KOi | K04521 |
OMAi | ELEDCGY |
OrthoDBi | 405736at2759 |
PhylomeDBi | P56817 |
TreeFami | TF329595 |
Family and domain databases
CDDi | cd05473 beta_secretase_like, 1 hit |
Gene3Di | 2.40.70.10, 2 hits |
InterProi | View protein in InterPro IPR001461 Aspartic_peptidase_A1 IPR001969 Aspartic_peptidase_AS IPR009119 BACE IPR009120 BACE1 IPR033874 Memapsin-like IPR033121 PEPTIDASE_A1 IPR021109 Peptidase_aspartic_dom_sf |
PANTHERi | PTHR13683 PTHR13683, 1 hit PTHR13683:SF245 PTHR13683:SF245, 1 hit |
Pfami | View protein in Pfam PF00026 Asp, 1 hit |
PRINTSi | PR01815 BACEFAMILY PR00792 PEPSIN |
SUPFAMi | SSF50630 SSF50630, 1 hit |
PROSITEi | View protein in PROSITE PS00141 ASP_PROTEASE, 1 hit PS51767 PEPTIDASE_A1, 1 hit |
s (6+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 6 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 6 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MAQALPWLLL WMGAGVLPAH GTQHGIRLPL RSGLGGAPLG LRLPRETDEE
60 70 80 90 100
PEEPGRRGSF VEMVDNLRGK SGQGYYVEMT VGSPPQTLNI LVDTGSSNFA
110 120 130 140 150
VGAAPHPFLH RYYQRQLSST YRDLRKGVYV PYTQGKWEGE LGTDLVSIPH
160 170 180 190 200
GPNVTVRANI AAITESDKFF INGSNWEGIL GLAYAEIARP DDSLEPFFDS
210 220 230 240 250
LVKQTHVPNL FSLQLCGAGF PLNQSEVLAS VGGSMIIGGI DHSLYTGSLW
260 270 280 290 300
YTPIRREWYY EVIIVRVEIN GQDLKMDCKE YNYDKSIVDS GTTNLRLPKK
310 320 330 340 350
VFEAAVKSIK AASSTEKFPD GFWLGEQLVC WQAGTTPWNI FPVISLYLMG
360 370 380 390 400
EVTNQSFRIT ILPQQYLRPV EDVATSQDDC YKFAISQSST GTVMGAVIME
410 420 430 440 450
GFYVVFDRAR KRIGFAVSAC HVHDEFRTAA VEGPFVTLDM EDCGYNIPQT
460 470 480 490 500
DESTLMTIAY VMAAICALFM LPLCLMVCQW RCLRCLRQQH DDFADDISLL
K
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketE9PJG7 | E9PJG7_HUMAN | Beta-secretase 1 | BACE1 | 467 | Annotation score: | ||
H0YDX0 | H0YDX0_HUMAN | Beta-secretase 1 | BACE1 | 40 | Annotation score: | ||
U3KPS1 | U3KPS1_HUMAN | Beta-secretase 1 | BACE1 | 51 | Annotation score: |
Sequence cautioni
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_060692 | 265 | V → A1 PublicationCorresponds to variant dbSNP:rs28989503Ensembl. | 1 | |
Natural variantiVAR_051509 | 481 | R → C. Corresponds to variant dbSNP:rs539765Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_047092 | 1 – 20 | MAQAL…VLPAH → MVPFIYLQAHFTLCSGWSST in isoform 5 and isoform 6. CuratedAdd BLAST | 20 | |
Alternative sequenceiVSP_047093 | 21 – 120 | Missing in isoform 5 and isoform 6. CuratedAdd BLAST | 100 | |
Alternative sequenceiVSP_005222 | 146 – 189 | Missing in isoform C and isoform D. 2 PublicationsAdd BLAST | 44 | |
Alternative sequenceiVSP_005223 | 190 – 214 | Missing in isoform B, isoform D and isoform 6. 2 PublicationsAdd BLAST | 25 |
Sequence databases
Genome annotation databases
Ensembli | ENST00000313005; ENSP00000318585; ENSG00000186318 [P56817-1] ENST00000392937; ENSP00000475405; ENSG00000186318 [P56817-5] ENST00000428381; ENSP00000402228; ENSG00000186318 [P56817-4] ENST00000445823; ENSP00000403685; ENSG00000186318 [P56817-3] ENST00000510630; ENSP00000422461; ENSG00000186318 [P56817-6] ENST00000513780; ENSP00000424536; ENSG00000186318 [P56817-2] |
GeneIDi | 23621 |
KEGGi | hsa:23621 |
UCSCi | uc001pqw.4 human [P56817-1] |
Keywords - Coding sequence diversityi
Alternative splicing, PolymorphismSimilar proteinsi
Cross-referencesi
Web resourcesi
NIEHS-SNPs |
Sequence databases
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1FKN | X-ray | 1.90 | A/B | 56-446 | [»] | |
1M4H | X-ray | 2.10 | A/B | 56-446 | [»] | |
1PY1 | X-ray | 2.60 | E/F/G/H | 494-501 | [»] | |
1SGZ | X-ray | 2.00 | A/B/C/D | 58-446 | [»] | |
1TQF | X-ray | 1.80 | A | 43-446 | [»] | |
1UJJ | X-ray | 2.60 | C | 490-501 | [»] | |
1UJK | X-ray | 1.90 | C/D | 490-501 | [»] | |
1W50 | X-ray | 1.75 | A | 43-453 | [»] | |
1W51 | X-ray | 2.55 | A | 43-453 | [»] | |
1XN2 | X-ray | 1.90 | A/B/C/D | 58-446 | [»] | |
1XN3 | X-ray | 2.00 | A/B/C/D | 58-446 | [»] | |
1XS7 | X-ray | 2.80 | D | 58-446 | [»] | |
1YM2 | X-ray | 2.05 | A/B/C | 48-447 | [»] | |
1YM4 | X-ray | 2.25 | A/B/C | 48-453 | [»] | |
2B8L | X-ray | 1.70 | A | 43-446 | [»] | |
2B8V | X-ray | 1.80 | A | 43-446 | [»] | |
2F3E | X-ray | 2.11 | A/B/C | 48-447 | [»] | |
2F3F | X-ray | 2.30 | A/B/C | 48-447 | [»] | |
2FDP | X-ray | 2.50 | A/B/C | 59-446 | [»] | |
2G94 | X-ray | 1.86 | A/B/C/D | 58-446 | [»] | |
2HIZ | X-ray | 2.50 | A/B/C | 14-453 | [»] | |
2HM1 | X-ray | 2.20 | A | 57-453 | [»] | |
2IQG | X-ray | 1.70 | A | 57-453 | [»] | |
2IRZ | X-ray | 1.80 | A | 43-446 | [»] | |
2IS0 | X-ray | 2.20 | A | 43-446 | [»] | |
2NTR | X-ray | 1.80 | A | 43-446 | [»] | |
2OAH | X-ray | 1.80 | A | 43-446 | [»] | |
2OF0 | X-ray | 2.25 | A | 45-446 | [»] | |
2OHK | X-ray | 2.20 | A | 45-446 | [»] | |
2OHL | X-ray | 2.65 | A | 45-446 | [»] | |
2OHM | X-ray | 2.70 | A | 45-446 | [»] | |
2OHN | X-ray | 2.15 | A | 45-446 | [»] | |
2OHP | X-ray | 2.25 | A | 45-446 | [»] | |
2OHQ | X-ray | 2.10 | A | 45-446 | [»] | |
2OHR | X-ray | 2.25 | A | 45-446 | [»] | |
2OHS | X-ray | 2.45 | A | 45-446 | [»] | |
2OHT | X-ray | 2.30 | A | 45-446 | [»] | |
2OHU | X-ray | 2.35 | A | 45-446 | [»] | |
2P4J | X-ray | 2.50 | A/B/C/D | 58-446 | [»] | |
2P83 | X-ray | 2.50 | A/B/C | 14-446 | [»] | |
2P8H | X-ray | 1.80 | A | 43-446 | [»] | |
2PH6 | X-ray | 2.00 | A | 43-446 | [»] | |
2PH8 | X-ray | 1.70 | A | 43-446 | [»] | |
2Q11 | X-ray | 2.40 | A/B/C | 59-446 | [»] | |
2Q15 | X-ray | 2.40 | A | 62-446 | [»] | |
2QK5 | X-ray | 2.20 | A/B | 55-447 | [»] | |
2QMD | X-ray | 1.65 | A/B | 55-447 | [»] | |
2QMF | X-ray | 1.75 | A/B | 55-447 | [»] | |
2QMG | X-ray | 1.89 | A/B | 55-447 | [»] | |
2QP8 | X-ray | 1.50 | A/B | 55-447 | [»] | |
2QU2 | X-ray | 2.60 | A | 46-454 | [»] | |
2QU3 | X-ray | 2.00 | A | 46-454 | [»] | |
2QZK | X-ray | 1.80 | A | 43-446 | [»] | |
2QZL | X-ray | 1.80 | A | 43-446 | [»] | |
2VA5 | X-ray | 2.75 | A | 14-453 | [»] | |
2VA6 | X-ray | 2.50 | A | 14-453 | [»] | |
2VA7 | X-ray | 2.20 | A | 14-453 | [»] | |
2VIE | X-ray | 1.90 | A | 61-452 | [»] | |
2VIJ | X-ray | 1.60 | A | 61-452 | [»] | |
2VIY | X-ray | 1.82 | A | 61-452 | [»] | |
2VIZ | X-ray | 1.60 | A | 61-452 | [»] | |
2VJ6 | X-ray | 1.80 | A | 61-452 | [»] | |
2VJ7 | X-ray | 1.60 | A | 61-452 | [»] | |
2VJ9 | X-ray | 1.60 | A | 61-452 | [»] | |
2VKM | X-ray | 2.05 | A/B/C/D | 58-446 | [»] | |
2VNM | X-ray | 1.79 | A | 61-452 | [»] | |
2VNN | X-ray | 1.87 | A | 61-452 | [»] | |
2WEZ | X-ray | 1.70 | A | 61-452 | [»] | |
2WF0 | X-ray | 1.60 | A | 61-452 | [»] | |
2WF1 | X-ray | 1.60 | A | 61-452 | [»] | |
2WF2 | X-ray | 1.80 | A | 61-452 | [»] | |
2WF3 | X-ray | 2.08 | A | 61-452 | [»] | |
2WF4 | X-ray | 1.80 | A | 61-452 | [»] | |
2WJO | X-ray | 2.50 | A | 58-460 | [»] | |
2XFI | X-ray | 1.73 | A | 61-452 | [»] | |
2XFJ | X-ray | 1.80 | A | 61-452 | [»] | |
2XFK | X-ray | 1.80 | A | 61-452 | [»] | |
2ZDZ | X-ray | 2.00 | A | 46-454 | [»] | |
2ZE1 | X-ray | 2.20 | A | 46-454 | [»] | |
2ZHR | X-ray | 2.50 | A/B | 45-454 | [»] | |
2ZHS | X-ray | 2.70 | A | 45-454 | [»] | |
2ZHT | X-ray | 2.35 | A | 45-454 | [»] | |
2ZHU | X-ray | 2.40 | A | 45-454 | [»] | |
2ZHV | X-ray | 1.85 | A | 45-454 | [»] | |
2ZJH | X-ray | 2.60 | A | 43-446 | [»] | |
2ZJI | X-ray | 2.30 | A | 43-446 | [»] | |
2ZJJ | X-ray | 2.20 | A | 43-446 | [»] | |
2ZJK | X-ray | 3.00 | A/B/C | 43-446 | [»] | |
2ZJL | X-ray | 2.10 | A | 43-446 | [»] | |
2ZJM | X-ray | 1.90 | A | 43-446 | [»] | |
2ZJN | X-ray | 2.70 | A | 43-446 | [»] | |
3BRA | X-ray | 2.30 | A | 46-454 | [»] | |
3BUF | X-ray | 2.30 | A | 46-454 | [»] | |
3BUG | X-ray | 2.50 | A | 46-454 | [»] | |
3BUH | X-ray | 2.30 | A | 46-454 | [»] | |
3CIB | X-ray | 1.72 | A/B | 58-447 | [»] | |
3CIC | X-ray | 1.75 | A/B | 58-447 | [»] | |
3CID | X-ray | 1.80 | A/B | 58-447 | [»] | |
3CKP | X-ray | 2.30 | A/B/C | 43-454 | [»] | |
3CKR | X-ray | 2.70 | A/B/C | 43-454 | [»] | |
3DM6 | X-ray | 2.60 | A/B/C | 42-446 | [»] | |
3DUY | X-ray | 1.97 | A/B/C | 48-447 | [»] | |
3DV1 | X-ray | 2.10 | A/B/C | 48-447 | [»] | |
3DV5 | X-ray | 2.10 | A/B/C | 48-447 | [»] | |
3EXO | X-ray | 2.10 | A | 43-454 | [»] | |
3FKT | X-ray | 1.90 | A | 43-446 | [»] | |
3H0B | X-ray | 2.70 | A/B/C | 43-446 | [»] | |
3HVG | X-ray | 2.26 | A/B/C | 46-453 | [»] | |
3HW1 | X-ray | 2.48 | A/B/C | 46-453 | [»] | |
3I25 | X-ray | 2.10 | A/B/C | 42-446 | [»] | |
3IGB | X-ray | 2.24 | A | 46-454 | [»] | |
3IN3 | X-ray | 2.00 | A | 46-454 | [»] | |
3IN4 | X-ray | 2.30 | A | 46-454 | [»] | |
3IND | X-ray | 2.25 | A | 46-454 | [»] | |
3INE | X-ray | 2.00 | A | 46-454 | [»] | |
3INF | X-ray | 1.85 | A | 46-454 | [»] | |
3INH | X-ray | 1.80 | A | 46-454 | [»] | |
3IVH | X-ray | 1.80 | A | 57-453 | [»] | |
3IVI | X-ray | 2.20 | A/B/C | 57-453 | [»] | |
3IXJ | X-ray | 2.20 | A/B/C | 59-446 | [»] | |
3IXK | X-ray | 2.50 | A/B/C | 42-446 | [»] | |
3K5C | X-ray | 2.12 | A/B/C | 48-447 | [»] | |
3K5D | X-ray | 2.90 | A/B/C | 48-453 | [»] | |
3K5F | X-ray | 2.25 | A/B/C | 48-447 | [»] | |
3K5G | X-ray | 2.00 | A/B/C | 48-447 | [»] | |
3KMX | X-ray | 1.70 | A/B | 53-447 | [»] | |
3KMY | X-ray | 1.90 | A/B | 53-447 | [»] | |
3KN0 | X-ray | 1.90 | A/B | 53-447 | [»] | |
3KYR | X-ray | 2.60 | A/B/C | 42-446 | [»] | |
3L38 | X-ray | 2.10 | A | 46-454 | [»] | |
3L3A | X-ray | 2.36 | A | 46-454 | [»] | |
3L58 | X-ray | 1.80 | A/B | 41-454 | [»] | |
3L59 | X-ray | 2.00 | A/B | 41-454 | [»] | |
3L5B | X-ray | 1.80 | A/B | 41-454 | [»] | |
3L5C | X-ray | 1.80 | A/B | 41-454 | [»] | |
3L5D | X-ray | 1.75 | A/B | 41-454 | [»] | |
3L5E | X-ray | 1.53 | A/B | 41-454 | [»] | |
3L5F | X-ray | 1.70 | A/B | 41-454 | [»] | |
3LHG | X-ray | 2.10 | A | 46-454 | [»] | |
3LNK | X-ray | 1.80 | A/B | 53-447 | [»] | |
3LPI | X-ray | 2.05 | A/B | 14-454 | [»] | |
3LPJ | X-ray | 1.79 | A/B | 14-454 | [»] | |
3LPK | X-ray | 1.93 | A/B | 14-454 | [»] | |
3MSJ | X-ray | 1.80 | A/B/C | 43-453 | [»] | |
3MSK | X-ray | 2.00 | A | 48-453 | [»] | |
3MSL | X-ray | 2.40 | A | 48-453 | [»] | |
3N4L | X-ray | 2.70 | A/B/C | 57-453 | [»] | |
3NSH | X-ray | 2.20 | A/B/C | 57-453 | [»] | |
3OHF | X-ray | 2.10 | A/B | 14-454 | [»] | |
3OHH | X-ray | 2.01 | A/B | 14-454 | [»] | |
3OOZ | X-ray | 1.80 | A | 46-454 | [»] | |
3PI5 | X-ray | 2.40 | A/B/C | 48-447 | [»] | |
3QBH | X-ray | 2.24 | A/B/C | 48-447 | [»] | |
3QI1 | X-ray | 2.30 | A | 57-453 | [»] | |
3R1G | X-ray | 2.80 | B | 57-453 | [»] | |
3R2F | X-ray | 2.53 | A/B/D/E | 14-454 | [»] | |
3RSV | X-ray | 2.50 | A | 43-453 | [»] | |
3RSX | X-ray | 2.48 | A | 43-453 | [»] | |
3RTH | X-ray | 2.70 | A | 43-453 | [»] | |
3RTM | X-ray | 2.76 | A | 43-453 | [»] | |
3RTN | X-ray | 2.70 | A | 43-453 | [»] | |
3RU1 | X-ray | 2.30 | A | 43-453 | [»] | |
3RVI | X-ray | 2.65 | A | 43-453 | [»] | |
3S2O | X-ray | 2.60 | A | 48-453 | [»] | |
3S7L | X-ray | 2.16 | A | 46-454 | [»] | |
3S7M | X-ray | 2.20 | A | 46-454 | [»] | |
3SKF | X-ray | 3.00 | A/B | 14-454 | [»] | |
3SKG | X-ray | 2.88 | A/B/D/E | 14-454 | [»] | |
3TPJ | X-ray | 1.61 | A | 43-454 | [»] | |
3TPL | X-ray | 2.50 | A/B/C | 43-454 | [»] | |
3TPP | X-ray | 1.60 | A | 43-454 | [»] | |
3TPR | X-ray | 2.55 | A | 43-454 | [»] | |
3U6A | X-ray | 2.20 | A/B/C | 58-446 | [»] | |
3UDH | X-ray | 1.70 | A | 58-453 | [»] | |
3UDJ | X-ray | 1.80 | A | 58-453 | [»] | |
3UDK | X-ray | 2.51 | A | 58-453 | [»] | |
3UDM | X-ray | 1.94 | A | 58-453 | [»] | |
3UDN | X-ray | 2.19 | A | 58-453 | [»] | |
3UDP | X-ray | 1.95 | A | 58-453 | [»] | |
3UDQ | X-ray | 2.73 | A | 58-453 | [»] | |
3UDR | X-ray | 1.95 | A | 58-453 | [»] | |
3UDY | X-ray | 2.00 | A | 58-453 | [»] | |
3UFL | X-ray | 1.90 | A | 58-446 | [»] | |
3UQP | X-ray | 1.77 | A | 43-454 | [»] | |
3UQR | X-ray | 3.06 | A/B/C | 43-454 | [»] | |
3UQU | X-ray | 1.70 | A | 43-454 | [»] | |
3UQW | X-ray | 2.20 | A | 43-454 | [»] | |
3UQX | X-ray | 1.70 | A | 43-454 | [»] | |
3VEU | X-ray | 1.52 | A | 48-447 | [»] | |
3VF3 | X-ray | 1.48 | A | 48-447 | [»] | |
3VG1 | X-ray | 1.77 | A | 48-447 | [»] | |
3VV6 | X-ray | 2.05 | A | 43-454 | [»] | |
3VV7 | X-ray | 2.10 | A | 43-454 | [»] | |
3VV8 | X-ray | 2.50 | A | 43-454 | [»] | |
3WB4 | X-ray | 2.25 | A | 43-454 | [»] | |
3WB5 | X-ray | 2.50 | A | 43-454 | [»] | |
3ZMG | X-ray | 1.74 | A | 46-454 | [»] | |
3ZOV | X-ray | 2.10 | A | 46-454 | [»] | |
4ACU | X-ray | 1.75 | A | 43-453 | [»] | |
4ACX | X-ray | 2.00 | A | 43-453 | [»] | |
4AZY | X-ray | 1.79 | A | 43-453 | [»] | |
4B00 | X-ray | 1.83 | A | 43-453 | [»] | |
4B05 | X-ray | 1.80 | A | 43-453 | [»] | |
4B0Q | X-ray | 1.87 | A | 62-445 | [»] | |
4B1C | X-ray | 1.95 | A | 58-445 | [»] | |
4B1D | X-ray | 1.95 | A | 58-445 | [»] | |
4B1E | X-ray | 1.95 | A | 58-445 | [»] | |
4B70 | X-ray | 1.60 | A | 61-445 | [»] | |
4B72 | X-ray | 1.60 | A | 58-445 | [»] | |
4B77 | X-ray | 1.80 | A | 58-445 | [»] | |
4B78 | X-ray | 1.50 | A | 62-445 | [»] | |
4BEK | X-ray | 2.39 | A | 46-454 | [»] | |
4BFD | X-ray | 2.30 | A | 46-454 | [»] | |
4D83 | X-ray | 2.40 | A/B/C | 48-447 | [»] | |
4D85 | X-ray | 2.65 | A | 48-453 | [»] | |
4D88 | X-ray | 1.70 | A | 48-447 | [»] | |
4D89 | X-ray | 1.65 | A | 48-447 | [»] | |
4D8C | X-ray | 2.07 | A/B/C | 48-447 | [»] | |
4DH6 | X-ray | 2.50 | A | 43-453 | [»] | |
4DI2 | X-ray | 2.00 | A/B/C | 43-453 | [»] | |
4DJU | X-ray | 1.80 | A/B | 41-454 | [»] | |
4DJV | X-ray | 1.73 | A/B | 41-454 | [»] | |
4DJW | X-ray | 1.90 | A/B | 41-454 | [»] | |
4DJX | X-ray | 1.50 | A/B | 41-454 | [»] | |
4DJY | X-ray | 1.86 | A/B | 41-454 | [»] | |
4DPF | X-ray | 1.80 | A | 57-446 | [»] | |
4DPI | X-ray | 1.90 | A | 57-446 | [»] | |
4DUS | X-ray | 2.50 | A | 43-453 | [»] | |
4DV9 | X-ray | 2.08 | A | 43-454 | [»] | |
4DVF | X-ray | 1.80 | A/B | 43-454 | [»] | |
4EWO | X-ray | 1.80 | A | 61-446 | [»] | |
4EXG | X-ray | 1.80 | A | 61-446 | [»] | |
4FCO | X-ray | 1.76 | A | 43-454 | [»] | |
4FGX | X-ray | 1.59 | A | 43-454 | [»] | |
4FM7 | X-ray | 1.56 | A | 58-453 | [»] | |
4FM8 | X-ray | 1.90 | A | 58-453 | [»] | |
4FRI | X-ray | 2.30 | A | 43-453 | [»] | |
4FRJ | X-ray | 1.95 | A | 43-453 | [»] | |
4FRK | X-ray | 2.10 | A | 43-453 | [»] | |
4FRS | X-ray | 1.70 | A/B | 53-447 | [»] | |
4FS4 | X-ray | 1.74 | A/B | 58-447 | [»] | |
4FSE | X-ray | 2.65 | A/B/D/E | 14-454 | [»] | |
4FSL | X-ray | 2.50 | A/B/D/E | 43-453 | [»] | |
4GID | X-ray | 2.00 | A/B/C/D | 59-446 | [»] | |
4GMI | X-ray | 1.80 | A | 57-446 | [»] | |
4H1E | X-ray | 1.90 | A/B | 41-454 | [»] | |
4H3F | X-ray | 1.70 | A/B | 41-454 | [»] | |
4H3G | X-ray | 1.85 | A/B | 41-454 | [»] | |
4H3I | X-ray | 1.96 | A/B | 41-454 | [»] | |
4H3J | X-ray | 1.60 | A/B | 41-454 | [»] | |
4HA5 | X-ray | 1.83 | A/B | 41-454 | [»] | |
4HZT | X-ray | 1.80 | A | 57-453 | [»] | |
4I0D | X-ray | 1.91 | A | 57-453 | [»] | |
4I0E | X-ray | 1.70 | A | 57-453 | [»] | |
4I0F | X-ray | 1.80 | A | 57-453 | [»] | |
4I0G | X-ray | 1.78 | A | 57-453 | [»] | |
4I0H | X-ray | 2.20 | A/B/C | 57-453 | [»] | |
4I0I | X-ray | 2.20 | A/B/C | 57-453 | [»] | |
4I0J | X-ray | 1.99 | A | 57-453 | [»] | |
4I0Z | X-ray | 1.80 | A | 57-453 | [»] | |
4I10 | X-ray | 2.07 | A | 57-453 | [»] | |
4I11 | X-ray | 1.89 | A | 57-453 | [»] | |
4I12 | X-ray | 1.78 | A | 57-453 | [»] | |
4I1C | X-ray | 2.00 | A | 57-453 | [»] | |
4IVS | X-ray | 2.64 | A | 43-454 | [»] | |
4IVT | X-ray | 1.60 | A | 43-454 | [»] | |
4J0P | X-ray | 1.97 | A | 46-454 | [»] | |
4J0T | X-ray | 2.05 | A | 46-454 | [»] | |
4J0V | X-ray | 1.94 | A | 46-454 | [»] | |
4J0Y | X-ray | 1.77 | A | 46-454 | [»] | |
4J0Z | X-ray | 2.13 | A | 46-454 | [»] | |
4J17 | X-ray | 1.81 | A | 46-454 | [»] | |
4J1C | X-ray | 2.01 | A | 46-454 | [»] | |
4J1E | X-ray | 1.78 | A | 46-454 | [»] | |
4J1F | X-ray | 2.25 | A | 46-454 | [»] | |
4J1H | X-ray | 2.20 | A | 46-454 | [»] | |
4J1I | X-ray | 2.05 | A | 46-454 | [»] | |
4J1K | X-ray | 2.18 | A | 46-454 | [»] | |
4JOO | X-ray | 1.80 | A | 57-453 | [»] | |
4JP9 | X-ray | 1.80 | A | 57-453 | [»] | |
4JPC | X-ray | 1.80 | A | 57-453 | [»] | |
4JPE | X-ray | 1.80 | A | 57-453 | [»] | |
4K8S | X-ray | 2.39 | A/B/C | 59-446 | [»] | |
4K9H | X-ray | 2.29 | A/B/C | 59-446 | [»] | |
4KE0 | X-ray | 2.30 | A/B/C | 43-453 | [»] | |
4KE1 | X-ray | 1.91 | A | 43-453 | [»] | |
4L7G | X-ray | 1.38 | A | 57-453 | [»] | |
4L7H | X-ray | 1.85 | A | 57-453 | [»] | |
4L7J | X-ray | 1.65 | A | 57-453 | [»] | |
4LC7 | X-ray | 1.70 | A | 57-453 | [»] | |
4LXA | X-ray | 1.95 | A/B/C | 48-447 | [»] | |
4LXK | X-ray | 2.05 | A/B/C | 48-447 | [»] | |
4LXM | X-ray | 2.30 | A/B/C | 48-447 | [»] | |
4N00 | X-ray | 1.80 | A | 57-453 | [»] | |
4PZW | X-ray | 1.80 | A | 57-453 | [»] | |
4PZX | X-ray | 1.80 | A | 57-453 | [»] | |
4R5N | X-ray | 1.80 | A | 57-453 | [»] | |
4R8Y | X-ray | 1.90 | A/B | 41-454 | [»] | |
4R91 | X-ray | 1.58 | A/B | 41-454 | [»] | |
4R92 | X-ray | 1.71 | A/B | 41-454 | [»] | |
4R93 | X-ray | 1.71 | A/B | 41-454 | [»] | |
4R95 | X-ray | 1.99 | A/B | 41-454 | [»] | |
4RCD | X-ray | 1.90 | A | 43-453 | [»] | |
4RCE | X-ray | 2.40 | A | 43-453 | [»] | |
4RCF | X-ray | 1.78 | A | 43-453 | [»] | |
4RRN | X-ray | 1.80 | A | 57-453 | [»] | |
4RRO | X-ray | 1.80 | A | 57-453 | [»] | |
4RRS | X-ray | 1.80 | A | 57-453 | [»] | |
4TRW | X-ray | 2.85 | A/B/C | 58-447 | [»] | |
4TRY | X-ray | 2.75 | A/B/C | 60-447 | [»] | |
4TRZ | X-ray | 3.25 | A/B/C | 60-447 | [»] | |
4WTU | X-ray | 1.85 | A | 43-453 | [»] | |
4WY1 | X-ray | 1.98 | A | 58-453 | [»] | |
4WY6 | X-ray | 2.10 | A | 46-454 | [»] | |
4X2L | X-ray | 2.55 | A | 46-454 | [»] | |
4X7I | X-ray | 1.77 | A/B | 14-454 | [»] | |
4XKX | X-ray | 1.80 | A | 43-453 | [»] | |
4XXS | X-ray | 1.86 | A | 46-454 | [»] | |
4YBI | X-ray | 1.84 | A/B | 14-454 | [»] | |
4ZPE | X-ray | 1.70 | A | 43-446 | [»] | |
4ZPF | X-ray | 1.80 | A | 43-446 | [»] | |
4ZPG | X-ray | 2.00 | A | 43-446 | [»] | |
4ZSM | X-ray | 1.96 | A/B | 14-454 | [»] | |
4ZSP | X-ray | 1.91 | A/B | 14-454 | [»] | |
4ZSQ | X-ray | 2.30 | A/B | 14-454 | [»] | |
4ZSR | X-ray | 1.65 | A/B | 14-454 | [»] | |
5CLM | X-ray | 2.61 | A | 46-446 | [»] | |
5DQC | X-ray | 2.47 | A/B/C | 58-447 | [»] | |
5ENK | X-ray | 2.11 | A | 14-454 | [»] | |
5ENM | X-ray | 1.98 | A | 14-454 | [»] | |
5EZX | X-ray | 1.90 | A | 57-446 | [»] | |
5EZZ | X-ray | 2.10 | A | 57-446 | [»] | |
5F00 | X-ray | 1.95 | A | 57-446 | [»] | |
5F01 | X-ray | 1.52 | A | 57-446 | [»] | |
5HD0 | X-ray | 1.65 | A/B | 41-454 | [»] | |
5HDU | X-ray | 1.58 | A/B | 41-454 | [»] | |
5HDV | X-ray | 1.71 | A/B | 41-454 | [»] | |
5HDX | X-ray | 1.60 | A/B | 41-454 | [»] | |
5HDZ | X-ray | 1.49 | A/B | 41-454 | [»] | |
5HE4 | X-ray | 1.53 | A/B | 41-454 | [»] | |
5HE5 | X-ray | 1.55 | A/B | 41-454 | [»] | |
5HE7 | X-ray | 1.71 | A/B | 41-454 | [»] | |
5HTZ | X-ray | 1.95 | A/B | 43-454 | [»] | |
5HU0 | X-ray | 1.83 | A/B | 43-454 | [»] | |
5HU1 | X-ray | 1.50 | A/B | 43-454 | [»] | |
5I3V | X-ray | 1.62 | A | 43-453 | [»] | |
5I3W | X-ray | 2.15 | A | 43-453 | [»] | |
5I3X | X-ray | 1.85 | A | 43-453 | [»] | |
5I3Y | X-ray | 2.15 | A | 43-453 | [»] | |
5IE1 | X-ray | 2.30 | A | 43-453 | [»] | |
5KQF | X-ray | 1.98 | A | 14-454 | [»] | |
5KR8 | X-ray | 2.12 | A | 14-454 | [»] | |
5MBW | X-ray | 2.95 | A | 46-454 | [»] | |
5MCO | X-ray | 2.49 | A | 46-454 | [»] | |
5MCQ | X-ray | 1.82 | A | 46-454 | [»] | |
5MXD | X-ray | 2.52 | A/B/C | 22-446 | [»] | |
5T1U | X-ray | 1.78 | A | 46-454 | [»] | |
5T1W | X-ray | 2.96 | A | 46-454 | [»] | |
5TOL | X-ray | 2.51 | A | 43-454 | [»] | |
5UYU | X-ray | 1.90 | A | 43-453 | [»] | |
5V0N | X-ray | 2.15 | A/B/C | 14-454 | [»] | |
5YGX | X-ray | 2.20 | A | 43-454 | [»] | |
5YGY | X-ray | 2.30 | A | 43-454 | [»] | |
6BFD | X-ray | 1.62 | A/B | 14-454 | [»] | |
6BFE | X-ray | 1.51 | A/B | 14-454 | [»] | |
6BFW | X-ray | 1.84 | A/B | 14-454 | [»] | |
6BFX | X-ray | 1.99 | A/B | 14-454 | [»] | |
6C2I | X-ray | 1.95 | A | 43-453 | [»] | |
6DHC | X-ray | 2.85 | A/B/C | 14-454 | [»] | |
6DMI | X-ray | 1.90 | A | 57-446 | [»] | |
6E3Z | X-ray | 1.94 | A/B/C | 22-446 | [»] | |
6EJ2 | X-ray | 1.46 | A | 1-501 | [»] | |
6EJ3 | X-ray | 1.94 | A | 1-501 | [»] | |
6EQM | X-ray | 1.35 | A | 48-447 | [»] | |
6FGY | X-ray | 1.54 | A | 60-453 | [»] | |
6JSE | X-ray | 2.00 | A | 43-454 | [»] | |
6JSF | X-ray | 2.30 | A | 43-454 | [»] | |
6JSG | X-ray | 2.30 | A | 43-454 | [»] | |
6JSN | X-ray | 2.60 | A | 43-454 | [»] | |
6OD6 | X-ray | 2.00 | A/B/C | 22-446 | [»] | |
SMRi | P56817 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGridi | 117154, 21 interactors |
CORUMi | P56817 |
DIPi | DIP-41388N |
IntActi | P56817, 40 interactors |
MINTi | P56817 |
STRINGi | 9606.ENSP00000318585 |
Chemistry databases
BindingDBi | P56817 |
ChEMBLi | CHEMBL4822 |
DrugBanki | DB07573 (2S)-1-(2,5-dimethylphenoxy)-3-morpholin-4-ylpropan-2-ol DB07736 (2S)-4-(4-fluorobenzyl)-N-(2-sulfanylethyl)piperazine-2-carboxamide DB07737 (2S)-4-(4-fluorobenzyl)-N-(3-sulfanylpropyl)piperazine-2-carboxamide DB07519 (6R)-2-amino-6-[2-(3'-methoxybiphenyl-3-yl)ethyl]-3,6-dimethyl-5,6-dihydropyrimidin-4(3H)-one DB07874 (6S)-2-amino-6-(3'-methoxybiphenyl-3-yl)-3,6-dimethyl-5,6-dihydropyrimidin-4(3H)-one DB07535 2-amino-6-[2-(1H-indol-6-yl)ethyl]pyrimidin-4(3H)-one DB08749 3-(2-AMINO-6-BENZOYLQUINAZOLIN-3(4H)-YL)-N-CYCLOHEXYL-N-METHYLPROPANAMIDE DB07345 4-(2-aminoethyl)-2-cyclohexylphenol DB07346 4-(2-aminoethyl)-2-ethylphenol DB07110 4-(4-FLUOROBENZYL)PIPERIDINE DB07415 4-[(1S)-1-(3-fluoro-4-methoxyphenyl)-2-(2-methoxy-5-nitrophenyl)ethyl]-1H-imidazol-2-amine DB07206 6-[2-(1H-INDOL-6-YL)ETHYL]PYRIDIN-2-AMINE DB07245 6-[2-(3'-METHOXYBIPHENYL-3-YL)ETHYL]PYRIDIN-2-AMINE DB06073 CTS-21166 DB02378 MMI-175 DB07734 N-(1-benzylpiperidin-4-yl)-4-sulfanylbutanamide DB07019 N-[(5R,14R)-5-AMINO-5,14-DIMETHYL-4-OXO-3-OXA-18-AZATRICYCLO[15.3.1.1~7,11~]DOCOSA-1(21),7(22),8,10,17,19-HEXAEN-19-YL]-N-METHYLMETHANESULFONAMIDE DB07735 N-[1-(2,6-dimethoxybenzyl)piperidin-4-yl]-4-sulfanylbutanamide DB07738 N-[1-(5-bromo-2,3-dimethoxybenzyl)piperidin-4-yl]-4-sulfanylbutanamide DB06930 N-[amino(imino)methyl]-2-(2,5-diphenyl-1H-pyrrol-1-yl)acetamide DB07089 N-[amino(imino)methyl]-2-[2-(2-chlorophenyl)-4-(4-propoxyphenyl)-3-thienyl]acetamide DB07175 N-{2-methyl-5-[(6-phenylpyrimidin-4-yl)amino]phenyl}methanesulfonamide DB07284 N~3~-(3-PYRIDIN-3-YLBENZYL)PYRIDINE-2,3-DIAMINE DB07993 N~3~-[3-(1H-INDOL-6-YL)BENZYL]PYRIDINE-2,3-DIAMINE DB07303 N~3~-[3-(5-METHOXYPYRIDIN-3-YL)BENZYL]PYRIDINE-2,3-DIAMINE DB07994 N~3~-[5-(1H-INDOL-6-YL)-2-(PYRIDIN-2-YLMETHOXY)BENZYL]PYRIDINE-2,3-DIAMINE DB07281 N~3~-BENZYLPYRIDINE-2,3-DIAMINE DB12285 Verubecestat |
DrugCentrali | P56817 |
GuidetoPHARMACOLOGYi | 2330 |
Protein family/group databases
MEROPSi | A01.004 |
TCDBi | 8.A.32.1.1 the Beta-amyloid cleaving enzyme (bace1) family |
PTM databases
GlyConnecti | 71 72 |
iPTMneti | P56817 |
PhosphoSitePlusi | P56817 |
SwissPalmi | P56817 |
UniCarbKBi | P56817 |
Polymorphism and mutation databases
BioMutai | BACE1 |
DMDMi | 296434407 |
Proteomic databases
jPOSTi | P56817 |
MassIVEi | P56817 |
PaxDbi | P56817 |
PeptideAtlasi | P56817 |
PRIDEi | P56817 |
ProteomicsDBi | 19820 43307 56947 [P56817-1] 56948 [P56817-2] 56949 [P56817-3] 56950 [P56817-4] |
Protocols and materials databases
ABCDi | P56817 |
DNASUi | 23621 |
Genome annotation databases
Ensembli | ENST00000313005; ENSP00000318585; ENSG00000186318 [P56817-1] ENST00000392937; ENSP00000475405; ENSG00000186318 [P56817-5] ENST00000428381; ENSP00000402228; ENSG00000186318 [P56817-4] ENST00000445823; ENSP00000403685; ENSG00000186318 [P56817-3] ENST00000510630; ENSP00000422461; ENSG00000186318 [P56817-6] ENST00000513780; ENSP00000424536; ENSG00000186318 [P56817-2] |
GeneIDi | 23621 |
KEGGi | hsa:23621 |
UCSCi | uc001pqw.4 human [P56817-1] |
Organism-specific databases
CTDi | 23621 |
DisGeNETi | 23621 |
GeneCardsi | BACE1 |
HGNCi | HGNC:933 BACE1 |
HPAi | CAB016358 |
MIMi | 604252 gene |
neXtProti | NX_P56817 |
OpenTargetsi | ENSG00000186318 |
PharmGKBi | PA25232 |
HUGEi | Search... |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG1339 Eukaryota ENOG410XNV7 LUCA |
GeneTreei | ENSGT00940000157786 |
InParanoidi | P56817 |
KOi | K04521 |
OMAi | ELEDCGY |
OrthoDBi | 405736at2759 |
PhylomeDBi | P56817 |
TreeFami | TF329595 |
Enzyme and pathway databases
BioCyci | MetaCyc:ENSG00000160610-MONOMER |
BRENDAi | 3.4.23.46 2681 |
Reactomei | R-HSA-977225 Amyloid fiber formation |
SABIO-RKi | P56817 |
SIGNORi | P56817 |
Miscellaneous databases
ChiTaRSi | BACE1 human |
EvolutionaryTracei | P56817 |
GeneWikii | Beta-secretase_1 |
GenomeRNAii | 23621 |
Pharosi | P56817 |
PMAP-CutDBi | P56817 |
PROi | PR:P56817 |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000186318 Expressed in 223 organ(s), highest expression level in C1 segment of cervical spinal cord |
ExpressionAtlasi | P56817 baseline and differential |
Genevisiblei | P56817 HS |
Family and domain databases
CDDi | cd05473 beta_secretase_like, 1 hit |
Gene3Di | 2.40.70.10, 2 hits |
InterProi | View protein in InterPro IPR001461 Aspartic_peptidase_A1 IPR001969 Aspartic_peptidase_AS IPR009119 BACE IPR009120 BACE1 IPR033874 Memapsin-like IPR033121 PEPTIDASE_A1 IPR021109 Peptidase_aspartic_dom_sf |
PANTHERi | PTHR13683 PTHR13683, 1 hit PTHR13683:SF245 PTHR13683:SF245, 1 hit |
Pfami | View protein in Pfam PF00026 Asp, 1 hit |
PRINTSi | PR01815 BACEFAMILY PR00792 PEPSIN |
SUPFAMi | SSF50630 SSF50630, 1 hit |
PROSITEi | View protein in PROSITE PS00141 ASP_PROTEASE, 1 hit PS51767 PEPTIDASE_A1, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | BACE1_HUMAN | |
Accessioni | P56817Primary (citable) accession number: P56817 Secondary accession number(s): A0M8W7 Q9ULS1 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 30, 2000 |
Last sequence update: | June 7, 2017 | |
Last modified: | November 13, 2019 | |
This is version 216 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 11
Human chromosome 11: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Peptidase families
Classification of peptidase families and list of entries - SIMILARITY comments
Index of protein domains and families - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references