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Protein

Glucoamylase

Gene

GLAA

Organism
Aspergillus awamori (Black koji mold)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose. EC:3.2.1.3

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei144Substrate1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei200Proton acceptorPROSITE-ProRule annotation1 Publication1
Active sitei203Proton donorPROSITE-ProRule annotation1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Polysaccharide degradation

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.2.1.3 494

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
CBM20 Carbohydrate-Binding Module Family 20
GH15 Glycoside Hydrolase Family 15

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Glucoamylase (EC:3.2.1.3)
Alternative name(s):
1,4-alpha-D-glucan glucohydrolase
Glucan 1,4-alpha-glucosidase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:GLAA
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiAspergillus awamori (Black koji mold)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri105351 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi144W → Y: 2% of wild-type activity. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 18Sequence analysisAdd BLAST18
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000000145919 – 246
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000146025 – 640GlucoamylaseAdd BLAST616

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>GlycosylationiCAR_000112195N-linked (GlcNAc...) asparagine1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi234 ↔ 2371 Publication
Disulfide bondi246 ↔ 4731 Publication
Disulfide bondi286 ↔ 2941 Publication
GlycosylationiCAR_000113419N-linked (GlcNAc...) asparagine1
Glycosylationi465O-linked (Man) serineBy similarity1
Glycosylationi467O-linked (Man) serine1
Glycosylationi468O-linked (Man) serine1
Glycosylationi476O-linked (Man) threonine1
Glycosylationi477O-linked (Man) serine1
Glycosylationi483O-linked (Man) serine1
Glycosylationi484O-linked (Man) serine1
Glycosylationi486O-linked (Man) threonine1
Glycosylationi488O-linked (Man) threonine1
Glycosylationi492O-linked (Man) serineBy similarity1
Glycosylationi496O-linked (Man) threonineBy similarity1
Glycosylationi499O-linked (Man) threonineBy similarity1
Glycosylationi500O-linked (Man) threonineBy similarity1
Glycosylationi501O-linked (Man) threonineBy similarity1
Glycosylationi502O-linked (Man) threonineBy similarity1
Glycosylationi504O-linked (Man) threonineBy similarity1
Glycosylationi506O-linked (Man) threonineBy similarity1
Glycosylationi508O-linked (Man) serineBy similarity1
Glycosylationi510O-linked (Man) serineBy similarity1
Glycosylationi512O-linked (Man) threonineBy similarity1
Glycosylationi513O-linked (Man) serineBy similarity1
Glycosylationi514O-linked (Man) threonineBy similarity1
Glycosylationi515O-linked (Man) serineBy similarity1
Glycosylationi517O-linked (Man) threonineBy similarity1
Glycosylationi518O-linked (Man) threonineBy similarity1
Glycosylationi520O-linked (Man) threonineBy similarity1
Glycosylationi522O-linked (Man) serineBy similarity1
Glycosylationi524O-linked (Man) threonineBy similarity1
Glycosylationi525O-linked (Man) serineBy similarity1
Glycosylationi526O-linked (Man) threonineBy similarity1
Glycosylationi527O-linked (Man) serineBy similarity1
Glycosylationi528O-linked (Man) threonineBy similarity1
Glycosylationi529O-linked (Man) serineBy similarity1
Glycosylationi530O-linked (Man) serineBy similarity1
Glycosylationi531O-linked (Man) threonineBy similarity1
Glycosylationi532O-linked (Man) serineBy similarity1
Glycosylationi534O-linked (Man) threonineBy similarity1
Glycosylationi535O-linked (Man) threonineBy similarity1

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

PTM databases

UniCarbKB; an annotated and curated database of glycan structures

More...
UniCarbKBi
P69327

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1640
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P69327

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P69327

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P69327

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini533 – 640CBM20PROSITE-ProRule annotationAdd BLAST108

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glycosyl hydrolase 15 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Conserved Domains Database

More...
CDDi
cd05811 CBM20_glucoamylase, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.50.10.10, 1 hit
2.60.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008928 6-hairpin_glycosidase_sf
IPR012341 6hp_glycosidase-like_sf
IPR013784 Carb-bd-like_fold
IPR034836 CBM20_glucoamylase
IPR002044 CBM_fam20
IPR011613 GH15-like
IPR000165 Glucoamylase
IPR008291 Glucoamylase_SBD
IPR013783 Ig-like_fold

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00686 CBM_20, 1 hit
PF00723 Glyco_hydro_15, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001031 Glu-a-glcsd_SBD, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00736 GLHYDRLASE15

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01065 CBM_2, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48208 SSF48208, 1 hit
SSF49452 SSF49452, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51166 CBM20, 1 hit
PS00820 GLUCOAMYLASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform G1 (identifier: P69327-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MSFRSLLALS GLVCTGLANV ISKRATLDSW LSNEATVART AILNNIGADG
60 70 80 90 100
AWVSGADSGI VVASPSTDNP DYFYTWTRDS GLVLKTLVDL FRNGDTSLLS
110 120 130 140 150
TIENYISAQA IVQGISNPSG DLSSGAGLGE PKFNVDETAY TGSWGRPQRD
160 170 180 190 200
GPALRATAMI GFGQWLLDNG YTSTATDIVW PLVRNDLSYV AQYWNQTGYD
210 220 230 240 250
LWEEVNGSSF FTIAVQHRAL VEGSAFATAV GSSCSWCDSQ APEILCYLQS
260 270 280 290 300
FWTGSFILAN FDSSRSGKDA NTLLGSIHTF DPEAACDDST FQPCSPRALA
310 320 330 340 350
NHKEVVDSFR SIYTLNDGLS DSEAVAVGRY PEDTYYNGNP WFLCTLAAAE
360 370 380 390 400
QLYDALYQWD KQGSLEVTDV SLDFFKALYS DAATGTYSSS SSTYSSIVDA
410 420 430 440 450
VKTFADGFVS IVETHAASNG SMSEQYDKSD GEQLSARDLT WSYAALLTAN
460 470 480 490 500
NRRNSVVPAS WGETSASSVP GTCAATSAIG TYSSVTVTSW PSIVATGGTT
510 520 530 540 550
TTATPTGSGS VTSTSKTTAT ASKTSTSTSS TSCTTPTAVA VTFDLTATTT
560 570 580 590 600
YGENIYLVGS ISQLGDWETS DGIALSADKY TSSDPLWYVT VTLPAGESFE
610 620 630 640
YKFIRIESDD SVEWESDPNR EYTVPQACGT STATVTDTWR
Length:640
Mass (Da):68,309
Last modified:November 1, 1986 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i26F58DD18AD7F702
GO
Isoform G2 (identifier: P69327-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     527-534: STSSTSCT → TTRSGMSL
     535-640: Missing.

Show »
Length:534
Mass (Da):56,730
Checksum:i94D188E946D0C12E
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_012836527 – 534STSSTSCT → TTRSGMSL in isoform G2. 1 Publication8
Alternative sequenceiVSP_000262535 – 640Missing in isoform G2. 1 PublicationAdd BLAST106

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
K02465 mRNA Translation: AAB59296.1
K02465 mRNA Translation: AAB59297.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A29166
A93066 A29776

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02465 mRNA Translation: AAB59296.1
K02465 mRNA Translation: AAB59297.1
PIRiA29166
A93066 A29776

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AGMX-ray2.30A25-495[»]
1DOGX-ray2.30A25-495[»]
1GAHX-ray2.00A25-496[»]
1GAIX-ray1.70A25-497[»]
1GLMX-ray2.40A25-495[»]
3GLYX-ray2.20A25-495[»]
ProteinModelPortaliP69327
SMRiP69327
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM20 Carbohydrate-Binding Module Family 20
GH15 Glycoside Hydrolase Family 15

PTM databases

UniCarbKBiP69327

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.3 494

Miscellaneous databases

EvolutionaryTraceiP69327

Family and domain databases

CDDicd05811 CBM20_glucoamylase, 1 hit
Gene3Di1.50.10.10, 1 hit
2.60.40.10, 1 hit
InterProiView protein in InterPro
IPR008928 6-hairpin_glycosidase_sf
IPR012341 6hp_glycosidase-like_sf
IPR013784 Carb-bd-like_fold
IPR034836 CBM20_glucoamylase
IPR002044 CBM_fam20
IPR011613 GH15-like
IPR000165 Glucoamylase
IPR008291 Glucoamylase_SBD
IPR013783 Ig-like_fold
PfamiView protein in Pfam
PF00686 CBM_20, 1 hit
PF00723 Glyco_hydro_15, 1 hit
PIRSFiPIRSF001031 Glu-a-glcsd_SBD, 1 hit
PRINTSiPR00736 GLHYDRLASE15
SMARTiView protein in SMART
SM01065 CBM_2, 1 hit
SUPFAMiSSF48208 SSF48208, 1 hit
SSF49452 SSF49452, 1 hit
PROSITEiView protein in PROSITE
PS51166 CBM20, 1 hit
PS00820 GLUCOAMYLASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAMYG_ASPAW
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P69327
Secondary accession number(s): P04064, Q92201, Q99179
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: December 5, 2018
This is version 80 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
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