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1VAH

Crystal structure of the pig pancreatic-amylase complexed with r-nitrophenyl-a-D-maltoside

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004556molecular_functionalpha-amylase activity
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005975biological_processcarbohydrate metabolic process
A0016052biological_processcarbohydrate catabolic process
A0016160molecular_functionamylase activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031404molecular_functionchloride ion binding
A0043169molecular_functioncation binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 498
ChainResidue
AARG195
AASN298
AARG337

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 500
ChainResidue
AASN100
AARG158
AASP167
AHIS201

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NPO A 701
ChainResidue
AASP300
AHOH587
ATRP59
AGLN63

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11412124","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11960990","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7897663","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8193143","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8681972","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8757803","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8994970","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9385631","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11412124","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11960990","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7897663","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8757803","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9385631","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P04746","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Pyrrolidone carboxylic acid","evidences":[{"source":"UniProtKB","id":"P04746","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP300
AASP197
AGLU233

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP197
AGLU233

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP236
AASP197

239492

PDB entries from 2025-07-30

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