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3AHY

Crystal structure of beta-glucosidase 2 from fungus Trichoderma reesei in complex with Tris

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008422molecular_functionbeta-glucosidase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0008422molecular_functionbeta-glucosidase activity
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005975biological_processcarbohydrate metabolic process
C0008422molecular_functionbeta-glucosidase activity
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0005975biological_processcarbohydrate metabolic process
D0008422molecular_functionbeta-glucosidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TRS A 500
ChainResidue
AGLN16
AHOH1058
AHOH1198
ATRP120
AGLU165
ATYR298
AGLU367
AGLU424
ATRP425
AHOH614
AHOH979

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE TRS B 500
ChainResidue
BGLN16
BTRP120
BGLU165
BTYR298
BGLU367
BTRP417
BGLU424
BTRP425
BHOH636
BHOH748
BHOH904
BHOH1281

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE TRS C 500
ChainResidue
CGLN16
CTRP120
CGLU165
CTYR298
CGLU367
CTRP417
CGLU424
CTRP425
CHOH685
CHOH714
CHOH928
CHOH1147

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TRS D 500
ChainResidue
DTRP120
DGLU165
DTYR298
DGLU367
DTRP417
DGLU424
DTRP425
DHOH613
DHOH671
DHOH1212

Functional Information from PROSITE/UniProt
site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FqWGfAtAAYQiEgA
ChainResidueDetails
APHE6-ALA20

223790

PDB entries from 2024-08-14

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