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6C9Z

THE CRYSTAL STRUCTURE OF THE alpha-Glucosidase (GH 31) W169Y mutant FROM RUMINOCOCCUS OBEUM ATCC 29174 in complex with voglibose

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 Residues13
Detailsbinding site for residue VOG A 701
ChainResidue
AASP73
AASP420
AHIS478
AHOH811
AHOH827
ATYR169
AASP197
AILE198
ATRP271
ATRP305
AASP307
AARG404
ATRP417

site_idAC2
Number of Residues15
Detailsbinding site for residue VOG B 701
ChainResidue
BASP73
BTYR169
BASP197
BILE198
BTRP271
BTRP305
BASP307
BARG404
BTRP417
BASP420
BPHE453
BHIS478
BHOH804
BHOH809
BHOH816

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 2024-07-31

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