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4XB3

Structure of dextran glucosidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000025biological_processmaltose catabolic process
A0004556molecular_functionalpha-amylase activity
A0004574molecular_functionoligo-1,6-glucosidase activity
A0004575molecular_functionsucrose alpha-glucosidase activity
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0005987biological_processsucrose catabolic process
A0006865biological_processamino acid transport
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0032450molecular_functionmaltose alpha-glucosidase activity
A0033934molecular_functionglucan 1,4-alpha-maltotriohydrolase activity
A0043896molecular_functionglucan 1,6-alpha-glucosidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CA A 601
ChainResidue
AASP148
AASP151
AGLU508
AHOH757

site_idAC2
Number of Residues7
Detailsbinding site for residue CA A 602
ChainResidue
AHOH1018
AHOH1020
AASP21
AASN23
AASP25
AILE27
AASP29

site_idAC3
Number of Residues7
Detailsbinding site for residue CA A 603
ChainResidue
ATHR417
AGLU516
AHOH713
AHOH720
AHOH726
AHOH727
AHOH729

site_idAC4
Number of Residues7
Detailsbinding site for residue CA A 604
ChainResidue
ATRP422
ALYS439
ASER441
AHOH702
AHOH714
AHOH721
AHOH736

site_idAC5
Number of Residues5
Detailsbinding site for residue P6G A 605
ChainResidue
ATRP5
AMET46
ALYS94
AILE188
AASP230

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
AASP194

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLN236

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
AASP313

219869

PDB entries from 2024-05-15

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