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6CA1

THE CRYSTAL STRUCTURE OF THE W169Y MUTANT OF ALPHA-GLUCOSIDASE (GH 31) FROM RUMINOCOCCUS OBEUM ATCC 29174 in complex with miglitol

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030246molecular_functioncarbohydrate binding
B0003824molecular_functioncatalytic activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030246molecular_functioncarbohydrate binding
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue MIG A 701
ChainResidue
ATRP169
AASP420
APHE453
AHIS478
AHOH807
AHOH903
AHOH1035
AASP197
AILE198
ATRP271
ATRP305
AASP307
AMET308
AARG404
ATRP417

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL A 702
ChainResidue
AASN561
AARG563
AHOH1002
BGLU46
BARG63
BHOH881

site_idAC3
Number of Residues15
Detailsbinding site for residue MIG B 701
ChainResidue
BTRP169
BASP197
BILE198
BTRP271
BTRP305
BASP307
BMET308
BARG404
BTRP417
BASP420
BPHE453
BHIS478
BHOH806
BHOH879
BHOH1061

site_idAC4
Number of Residues6
Detailsbinding site for residue GOL B 702
ChainResidue
AGLU46
AARG63
AHOH956
BASN561
BARG563
BHOH886

Functional Information from PROSITE/UniProt
site_idPS00129
Number of Residues8
DetailsGLYCOSYL_HYDROL_F31_1 Glycosyl hydrolases family 31 active site. GFWnDMNE
ChainResidueDetails
AGLY303-GLU310

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PDB entries from 2024-10-09

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