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2JKP

Structure of a family 97 alpha-glucosidase from Bacteroides thetaiotaomicron in complex with castanospermine

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004339molecular_functionglucan 1,4-alpha-glucosidase activity
A0004558molecular_functionalpha-1,4-glucosidase activity
A0005509molecular_functioncalcium ion binding
A0005886cellular_componentplasma membrane
A0005983biological_processstarch catabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030246molecular_functioncarbohydrate binding
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
B0000272biological_processpolysaccharide catabolic process
B0004339molecular_functionglucan 1,4-alpha-glucosidase activity
B0004558molecular_functionalpha-1,4-glucosidase activity
B0005509molecular_functioncalcium ion binding
B0005886cellular_componentplasma membrane
B0005983biological_processstarch catabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030246molecular_functioncarbohydrate binding
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE CTS A1727
ChainResidue
ATRP331
AVAL471
AHIS507
AGLU508
AGLU526
AGLU532
ACA1728
AHOH2434
AHOH2519
AHOH2527
AILE335
ATRP341
AGLU391
ATRP397
ATRP400
AHIS437
AGLU439
ALYS467

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE CTS B1727
ChainResidue
BTRP331
BILE335
BTRP341
BGLU391
BTRP397
BTRP400
BHIS437
BGLU439
BLYS467
BVAL471
BHIS507
BGLU508
BGLU526
BGLU532
BCA1728
BHOH2447
BHOH2598

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B1728
ChainResidue
BGLU194
BGLU508
BGLU526
BGLU532
BCTS1727
BHOH2144

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A1728
ChainResidue
AGLU194
AGLU508
AGLU526
AGLU532
ACTS1727
AHOH2527

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A1729
ChainResidue
APRO112
AVAL113
ATRP114
ACYS516
APRO520
AHOH2090
AHOH2656

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A1730
ChainResidue
AASP333
ALYS338
AASN372
ATYR376
AILE603

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B1729
ChainResidue
BPRO112
BVAL113
BTRP114
BCYS516
BPRO520
BHOH2064
BHOH2599

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B1730
ChainResidue
BASP333
BLYS338
BASN372
BTYR376

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"18981178","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18981178","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsSite: {"description":"Substrate"}
ChainResidueDetails

242500

PDB entries from 2025-10-01

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