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P00811

- AMPC_ECOLI

UniProt

P00811 - AMPC_ECOLI

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Protein

Beta-lactamase

Gene
ampC, ampA, b4150, JW4111
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.

Catalytic activityi

A beta-lactam + H2O = a substituted beta-amino acid.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei80 – 801Acyl-ester intermediate1 Publication
Active sitei166 – 1661Proton acceptor

GO - Molecular functioni

  1. beta-lactamase activity Source: EcoliWiki

GO - Biological processi

  1. antibiotic catabolic process Source: InterPro
  2. response to antibiotic Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antibiotic resistance

Enzyme and pathway databases

BioCyciEcoCyc:EG10040-MONOMER.
ECOL316407:JW4111-MONOMER.
MetaCyc:EG10040-MONOMER.
SABIO-RKP00811.

Protein family/group databases

MEROPSiS12.006.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-lactamase (EC:3.5.2.6)
Alternative name(s):
Cephalosporinase
Gene namesi
Name:ampC
Synonyms:ampA
Ordered Locus Names:b4150, JW4111
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10040. ampC.

Subcellular locationi

GO - Cellular componenti

  1. outer membrane-bounded periplasmic space Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi80 – 801S → D, E or G: Loss of activity. 1 Publication
Mutagenesisi83 – 831K → Q or T: Lowers activity more than 1000-fold and increases protein stability. 1 Publication
Mutagenesisi166 – 1661Y → E: Lowers activity more than 1000-fold. 1 Publication
Mutagenesisi168 – 1681N → D or H: Lowers activity more than 1000-fold. 1 Publication
Mutagenesisi331 – 3311K → A: Lowers activity more than 1000-fold. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 377358Beta-lactamasePRO_0000016958Add
BLAST

2D gel databases

SWISS-2DPAGEP00811.

PTM databases

PhosSiteiP0809371.

Expressioni

Gene expression databases

GenevestigatoriP00811.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

IntActiP00811. 1 interaction.
STRINGi511145.b4150.

Structurei

Secondary structure

1
377
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi22 – 3918
Beta strandi42 – 509
Beta strandi53 – 6311
Turni64 – 674
Beta strandi75 – 773
Helixi79 – 813
Helixi82 – 9514
Helixi105 – 1084
Helixi115 – 1173
Helixi122 – 1265
Helixi144 – 15310
Beta strandi162 – 1643
Helixi168 – 17811
Turni179 – 1835
Helixi186 – 1938
Turni194 – 1996
Beta strandi204 – 2063
Helixi209 – 2146
Beta strandi218 – 2203
Beta strandi223 – 2253
Turni229 – 2313
Helixi233 – 2364
Beta strandi240 – 2423
Helixi243 – 25412
Helixi256 – 2583
Helixi262 – 27110
Beta strandi273 – 2786
Beta strandi281 – 2833
Beta strandi288 – 2936
Helixi296 – 3016
Beta strandi303 – 3053
Beta strandi306 – 3083
Beta strandi310 – 3134
Beta strandi315 – 3217
Beta strandi325 – 33511
Beta strandi338 – 3458
Helixi346 – 3483
Beta strandi350 – 3589
Helixi362 – 37615

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C3BX-ray2.25A/B20-377[»]
1FCMX-ray2.46A/B20-377[»]
1FCNX-ray2.35A/B20-377[»]
1FCOX-ray2.20A/B20-377[»]
1FSWX-ray1.90A/B20-376[»]
1FSYX-ray1.75A/B20-376[»]
1GA9X-ray2.10A/B20-377[»]
1I5QX-ray1.83A/B20-377[»]
1IELX-ray2.00A/B20-377[»]
1IEMX-ray2.30A/B20-377[»]
1KDSX-ray2.15A/B20-377[»]
1KDWX-ray2.28A/B20-377[»]
1KE0X-ray2.30A/B20-377[»]
1KE3X-ray2.15A/B20-377[»]
1KE4X-ray1.72A/B20-377[»]
1KVLX-ray1.53A/B20-377[»]
1KVMX-ray2.06A/B20-377[»]
1L0DX-ray1.53A/B20-377[»]
1L0EX-ray1.90A/B20-377[»]
1L0FX-ray1.66A/B20-377[»]
1L0GX-ray1.50A/B20-377[»]
1L2SX-ray1.94A/B20-377[»]
1LL5X-ray1.80A/B20-377[»]
1LL9X-ray1.87A/B20-377[»]
1LLBX-ray1.72A/B20-377[»]
1MXOX-ray1.83A/B20-377[»]
1MY8X-ray1.72A/B20-377[»]
1O07X-ray1.71A/B20-377[»]
1PI4X-ray1.39A/B20-377[»]
1PI5X-ray1.49A/B20-377[»]
1XGIX-ray1.96A/B20-377[»]
1XGJX-ray1.97A/B20-377[»]
2BLSX-ray2.00A/B20-377[»]
2FFYX-ray1.07A/B20-377[»]
2HDQX-ray2.10A/B20-377[»]
2HDRX-ray2.20A/B20-377[»]
2HDSX-ray1.16A/B20-377[»]
2HDUX-ray1.49A/B20-377[»]
2I72X-ray2.20A/B20-377[»]
2P9VX-ray1.80A/B20-377[»]
2PU2X-ray1.86A/B20-377[»]
2PU4X-ray2.00A/B20-377[»]
2R9WX-ray1.80A/B20-377[»]
2R9XX-ray1.90A/B20-377[»]
2RCXX-ray2.00A/B20-377[»]
3BLSX-ray2.30A/B20-377[»]
3BM6X-ray2.10A/B20-377[»]
3FKVX-ray1.85A/B20-377[»]
3FKWX-ray1.50A/B20-377[»]
3GQZX-ray1.80A/B20-377[»]
3GR2X-ray1.80A/B20-377[»]
3GRJX-ray2.49A/B20-377[»]
3GSGX-ray2.10A/B20-377[»]
3GTCX-ray1.90A/B20-377[»]
3GV9X-ray1.80A/B20-377[»]
3GVBX-ray1.80A/B20-377[»]
3IWIX-ray1.64A/B20-377[»]
3IWOX-ray1.90A/B20-377[»]
3IWQX-ray1.84A/B20-377[»]
3IXBX-ray1.63A/B20-377[»]
3IXDX-ray2.64A/B20-377[»]
3IXGX-ray2.14A/B20-377[»]
3IXHX-ray2.30A/B20-377[»]
3O86X-ray1.60A/B20-377[»]
3O87X-ray1.78A/B20-377[»]
3O88X-ray1.64A/B20-377[»]
4E3IX-ray1.60A/B20-377[»]
4E3JX-ray1.80A/B20-377[»]
4E3KX-ray1.43A/B20-377[»]
4E3LX-ray1.43A/B20-377[»]
4E3MX-ray1.44A/B20-377[»]
4E3NX-ray1.49A/B20-377[»]
4E3OX-ray1.60A/B20-377[»]
4JXSX-ray1.90A/B20-377[»]
4JXVX-ray1.76A/B20-377[»]
4JXWX-ray2.30A/B20-377[»]
4KZ3X-ray1.67A/B20-377[»]
4KZ4X-ray1.42A/B20-377[»]
4KZ5X-ray1.35A/B20-377[»]
4KZ6X-ray1.68A/B20-377[»]
4KZ7X-ray1.43A/B20-377[»]
4KZ8X-ray2.28A/B20-377[»]
4KZ9X-ray1.72A/B20-377[»]
4KZAX-ray1.60A/B20-377[»]
4KZBX-ray1.37A/B20-377[»]
4OKPX-ray1.37A/B20-377[»]
4OLDX-ray1.48A/B20-377[»]
4OLGX-ray1.71A/B20-377[»]
ProteinModelPortaliP00811.
SMRiP00811. Positions 20-377.

Miscellaneous databases

EvolutionaryTraceiP00811.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni331 – 3333Substrate binding By similarity

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1680.
HOGENOMiHOG000267102.
KOiK01467.
OMAiKVGDMTQ.
OrthoDBiEOG60SCH1.
PhylomeDBiP00811.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
IPR001586. Beta-lactam_class-C_AS.
[Graphical view]
PfamiPF00144. Beta-lactamase. 1 hit.
[Graphical view]
SUPFAMiSSF56601. SSF56601. 1 hit.
PROSITEiPS00336. BETA_LACTAMASE_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00811-1 [UniParc]FASTAAdd to Basket

« Hide

MFKTTLCALL ITASCSTFAA PQQINDIVHR TITPLIEQQK IPGMAVAVIY    50
QGKPYYFTWG YADIAKKQPV TQQTLFELGS VSKTFTGVLG GDAIARGEIK 100
LSDPTTKYWP ELTAKQWNGI TLLHLATYTA GGLPLQVPDE VKSSSDLLRF 150
YQNWQPAWAP GTQRLYANSS IGLFGALAVK PSGLSFEQAM QTRVFQPLKL 200
NHTWINVPPA EEKNYAWGYR EGKAVHVSPG ALDAEAYGVK STIEDMARWV 250
QSNLKPLDIN EKTLQQGIQL AQSRYWQTGD MYQGLGWEML DWPVNPDSII 300
NGSDNKIALA ARPVKAITPP TPAVRASWVH KTGATGGFGS YVAFIPEKEL 350
GIVMLANKNY PNPARVDAAW QILNALQ 377
Length:377
Mass (Da):41,556
Last modified:July 21, 1986 - v1
Checksum:i3C6FB4FE4EF96C9F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J01611 Genomic DNA. Translation: AAA23441.1.
U14003 Genomic DNA. Translation: AAA97049.1.
U00096 Genomic DNA. Translation: AAC77110.1.
AP009048 Genomic DNA. Translation: BAE78154.1.
V00277 Genomic DNA. Translation: CAA23537.1.
PIRiA01007. QKEC.
RefSeqiNP_418574.1. NC_000913.3.
YP_492295.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC77110; AAC77110; b4150.
BAE78154; BAE78154; BAE78154.
GeneIDi12932283.
948669.
KEGGiecj:Y75_p4039.
eco:b4150.
PATRICi32123873. VBIEscCol129921_4284.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J01611 Genomic DNA. Translation: AAA23441.1 .
U14003 Genomic DNA. Translation: AAA97049.1 .
U00096 Genomic DNA. Translation: AAC77110.1 .
AP009048 Genomic DNA. Translation: BAE78154.1 .
V00277 Genomic DNA. Translation: CAA23537.1 .
PIRi A01007. QKEC.
RefSeqi NP_418574.1. NC_000913.3.
YP_492295.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1C3B X-ray 2.25 A/B 20-377 [» ]
1FCM X-ray 2.46 A/B 20-377 [» ]
1FCN X-ray 2.35 A/B 20-377 [» ]
1FCO X-ray 2.20 A/B 20-377 [» ]
1FSW X-ray 1.90 A/B 20-376 [» ]
1FSY X-ray 1.75 A/B 20-376 [» ]
1GA9 X-ray 2.10 A/B 20-377 [» ]
1I5Q X-ray 1.83 A/B 20-377 [» ]
1IEL X-ray 2.00 A/B 20-377 [» ]
1IEM X-ray 2.30 A/B 20-377 [» ]
1KDS X-ray 2.15 A/B 20-377 [» ]
1KDW X-ray 2.28 A/B 20-377 [» ]
1KE0 X-ray 2.30 A/B 20-377 [» ]
1KE3 X-ray 2.15 A/B 20-377 [» ]
1KE4 X-ray 1.72 A/B 20-377 [» ]
1KVL X-ray 1.53 A/B 20-377 [» ]
1KVM X-ray 2.06 A/B 20-377 [» ]
1L0D X-ray 1.53 A/B 20-377 [» ]
1L0E X-ray 1.90 A/B 20-377 [» ]
1L0F X-ray 1.66 A/B 20-377 [» ]
1L0G X-ray 1.50 A/B 20-377 [» ]
1L2S X-ray 1.94 A/B 20-377 [» ]
1LL5 X-ray 1.80 A/B 20-377 [» ]
1LL9 X-ray 1.87 A/B 20-377 [» ]
1LLB X-ray 1.72 A/B 20-377 [» ]
1MXO X-ray 1.83 A/B 20-377 [» ]
1MY8 X-ray 1.72 A/B 20-377 [» ]
1O07 X-ray 1.71 A/B 20-377 [» ]
1PI4 X-ray 1.39 A/B 20-377 [» ]
1PI5 X-ray 1.49 A/B 20-377 [» ]
1XGI X-ray 1.96 A/B 20-377 [» ]
1XGJ X-ray 1.97 A/B 20-377 [» ]
2BLS X-ray 2.00 A/B 20-377 [» ]
2FFY X-ray 1.07 A/B 20-377 [» ]
2HDQ X-ray 2.10 A/B 20-377 [» ]
2HDR X-ray 2.20 A/B 20-377 [» ]
2HDS X-ray 1.16 A/B 20-377 [» ]
2HDU X-ray 1.49 A/B 20-377 [» ]
2I72 X-ray 2.20 A/B 20-377 [» ]
2P9V X-ray 1.80 A/B 20-377 [» ]
2PU2 X-ray 1.86 A/B 20-377 [» ]
2PU4 X-ray 2.00 A/B 20-377 [» ]
2R9W X-ray 1.80 A/B 20-377 [» ]
2R9X X-ray 1.90 A/B 20-377 [» ]
2RCX X-ray 2.00 A/B 20-377 [» ]
3BLS X-ray 2.30 A/B 20-377 [» ]
3BM6 X-ray 2.10 A/B 20-377 [» ]
3FKV X-ray 1.85 A/B 20-377 [» ]
3FKW X-ray 1.50 A/B 20-377 [» ]
3GQZ X-ray 1.80 A/B 20-377 [» ]
3GR2 X-ray 1.80 A/B 20-377 [» ]
3GRJ X-ray 2.49 A/B 20-377 [» ]
3GSG X-ray 2.10 A/B 20-377 [» ]
3GTC X-ray 1.90 A/B 20-377 [» ]
3GV9 X-ray 1.80 A/B 20-377 [» ]
3GVB X-ray 1.80 A/B 20-377 [» ]
3IWI X-ray 1.64 A/B 20-377 [» ]
3IWO X-ray 1.90 A/B 20-377 [» ]
3IWQ X-ray 1.84 A/B 20-377 [» ]
3IXB X-ray 1.63 A/B 20-377 [» ]
3IXD X-ray 2.64 A/B 20-377 [» ]
3IXG X-ray 2.14 A/B 20-377 [» ]
3IXH X-ray 2.30 A/B 20-377 [» ]
3O86 X-ray 1.60 A/B 20-377 [» ]
3O87 X-ray 1.78 A/B 20-377 [» ]
3O88 X-ray 1.64 A/B 20-377 [» ]
4E3I X-ray 1.60 A/B 20-377 [» ]
4E3J X-ray 1.80 A/B 20-377 [» ]
4E3K X-ray 1.43 A/B 20-377 [» ]
4E3L X-ray 1.43 A/B 20-377 [» ]
4E3M X-ray 1.44 A/B 20-377 [» ]
4E3N X-ray 1.49 A/B 20-377 [» ]
4E3O X-ray 1.60 A/B 20-377 [» ]
4JXS X-ray 1.90 A/B 20-377 [» ]
4JXV X-ray 1.76 A/B 20-377 [» ]
4JXW X-ray 2.30 A/B 20-377 [» ]
4KZ3 X-ray 1.67 A/B 20-377 [» ]
4KZ4 X-ray 1.42 A/B 20-377 [» ]
4KZ5 X-ray 1.35 A/B 20-377 [» ]
4KZ6 X-ray 1.68 A/B 20-377 [» ]
4KZ7 X-ray 1.43 A/B 20-377 [» ]
4KZ8 X-ray 2.28 A/B 20-377 [» ]
4KZ9 X-ray 1.72 A/B 20-377 [» ]
4KZA X-ray 1.60 A/B 20-377 [» ]
4KZB X-ray 1.37 A/B 20-377 [» ]
4OKP X-ray 1.37 A/B 20-377 [» ]
4OLD X-ray 1.48 A/B 20-377 [» ]
4OLG X-ray 1.71 A/B 20-377 [» ]
ProteinModelPortali P00811.
SMRi P00811. Positions 20-377.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P00811. 1 interaction.
STRINGi 511145.b4150.

Chemistry

BindingDBi P00811.
ChEMBLi CHEMBL2026.
DrugBanki DB00456. Cefalotin.
DB01147. Cloxacillin.

Protein family/group databases

MEROPSi S12.006.

PTM databases

PhosSitei P0809371.

2D gel databases

SWISS-2DPAGE P00811.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC77110 ; AAC77110 ; b4150 .
BAE78154 ; BAE78154 ; BAE78154 .
GeneIDi 12932283.
948669.
KEGGi ecj:Y75_p4039.
eco:b4150.
PATRICi 32123873. VBIEscCol129921_4284.

Organism-specific databases

EchoBASEi EB0038.
EcoGenei EG10040. ampC.

Phylogenomic databases

eggNOGi COG1680.
HOGENOMi HOG000267102.
KOi K01467.
OMAi KVGDMTQ.
OrthoDBi EOG60SCH1.
PhylomeDBi P00811.

Enzyme and pathway databases

BioCyci EcoCyc:EG10040-MONOMER.
ECOL316407:JW4111-MONOMER.
MetaCyc:EG10040-MONOMER.
SABIO-RK P00811.

Miscellaneous databases

EvolutionaryTracei P00811.
PROi P00811.

Gene expression databases

Genevestigatori P00811.

Family and domain databases

Gene3Di 3.40.710.10. 1 hit.
InterProi IPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
IPR001586. Beta-lactam_class-C_AS.
[Graphical view ]
Pfami PF00144. Beta-lactamase. 1 hit.
[Graphical view ]
SUPFAMi SSF56601. SSF56601. 1 hit.
PROSITEi PS00336. BETA_LACTAMASE_C. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "ampC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of beta-lactamases of the penicillinase type."
    Jaurin B., Grundstroem T.
    Proc. Natl. Acad. Sci. U.S.A. 78:4897-4901(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 20-31.
    Strain: K12.
  2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Overlap between ampC and frd operons on the Escherichia coli chromosome."
    Grundstroem T., Jaurin B.
    Proc. Natl. Acad. Sci. U.S.A. 79:1111-1115(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
  6. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  7. "Three-dimensional structure of AmpC beta-lactamase from Escherichia coli bound to a transition-state analogue: possible implications for the oxyanion hypothesis and for inhibitor design."
    Usher K.C., Blaszczak L.C., Weston G.S., Shoichet B.K., Remington S.J.
    Biochemistry 37:16082-16092(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  8. "The complexed structure and antimicrobial activity of a non-beta-lactam inhibitor of AmpC beta-lactamase."
    Powers R.A., Blazquez J., Weston G.S., Morosini M.I., Baquero F., Shoichet B.K.
    Protein Sci. 8:2330-2337(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
  9. "Structures of ceftazidime and its transition-state analogue in complex with AmpC beta-lactamase: implications for resistance mutations and inhibitor design."
    Powers R.A., Caselli E., Focia P.J., Prati F., Shoichet B.K.
    Biochemistry 40:9207-9214(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGUE.
  10. "Structural bases of stability-function tradeoffs in enzymes."
    Beadle B.M., Shoichet B.K.
    J. Mol. Biol. 321:285-296(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS), MUTAGENESIS OF SER-80; LYS-83; TYR-166; ASN-168 AND LYS-331.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).

Entry informationi

Entry nameiAMPC_ECOLI
AccessioniPrimary (citable) accession number: P00811
Secondary accession number(s): Q2M6F2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: September 3, 2014
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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