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1AGM

Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. x100 to 2.4 angstroms resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004339molecular_functionglucan 1,4-alpha-glucosidase activity
A0005975biological_processcarbohydrate metabolic process
A0005976biological_processpolysaccharide metabolic process
Functional Information from PDB Data
site_idSB1
Number of Residues7
DetailsSUBSITE 1 OF THE ACTIVE SITE
ChainResidue
AARG54
AASP55
ALEU177
AGLU179
AARG305
AGLU400
AHOH500

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKSDGDELSarDL
ChainResidueDetails
AASP403-LEU415

site_idPS00820
Number of Residues11
DetailsGLUCOAMYLASE Glucoamylase active site region signature. TGy.DlWEEvnG
ChainResidueDetails
ATHR173-GLY183

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10051","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1970434","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10051","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1970434","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000112"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000113"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (Man) serine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues5
DetailsGlycosylation: {"description":"O-linked (Man) serine"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsGlycosylation: {"description":"O-linked (Man) threonine"}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 393
ChainResidueDetails
ATRP120transition state stabiliser
AASP176proton shuttle (general acid/base), transition state stabiliser
AGLU179proton shuttle (general acid/base)
AGLU180activator
AGLU400activator

site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 8195212, 8535779
ChainResidueDetails
ATRP120
AGLU179
AGLU400

246905

PDB entries from 2025-12-31

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