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3VIP

Crystal structure of beta-glucosidase from termite Neotermes koshunensis in complex with a new glucopyranosidic product

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008422molecular_functionbeta-glucosidase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0102483molecular_functionobsolete scopolin beta-glucosidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE GOI A 507
ChainResidue
AGLN45
AGLU402
ATRP444
AGLU451
ATRP452
APHE460
AONB508
AHOH1114
AHOH1190
AHIS148
AASN192
AASP193
ATHR196
ATYR337
AGLN363
ASER373
ATRP374

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ONB A 508
ChainResidue
AGLU288
AGLU347
AGLY348
ATYR349
AGOI507
AHOH555

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 509
ChainResidue
AASN303
AGLU307
AGLU350
AARG355
AHOH765
AHOH1007

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 510
ChainResidue
ALYS179
AASN180
AHOH833
AHOH949

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 511
ChainResidue
AHOH606
AHOH1062
AHOH1062

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 512
ChainResidue
AASN262
AASN262

Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. VFITENGFS
ChainResidueDetails
AVAL398-SER406

226707

PDB entries from 2024-10-30

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