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3APG

Crystal structure of hyperthermophilic beta-glucosidase from pyrococcus furiosus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005975biological_processcarbohydrate metabolic process
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0005975biological_processcarbohydrate metabolic process
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 473
ChainResidue
AGLN17
AHIS150
AASN206
AGLU207
AGLU372
ATRP410
AGLU417
ATRP418

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 473
ChainResidue
BHIS150
BASN206
BGLU207
BGLU372
BTRP410
BGLU417
BTRP418
BGLN17

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 474
ChainResidue
AGLU128
AARG131
ASER135
BGLU128
BARG131
BSER135

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL C 473
ChainResidue
CGLN17
CHIS150
CASN206
CGLU207
CGLU372
CTRP410
CGLU417
CTRP418

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL D 473
ChainResidue
DGLN17
DHIS150
DASN206
DGLU207
DGLU372
DTRP410
DGLU417
DTRP418

Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. MIITENGMA
ChainResidueDetails
AMET368-ALA376

site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FmFGySwSGFQfEmG
ChainResidueDetails
APHE7-GLY21

223532

PDB entries from 2024-08-07

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