Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6QWI

Structure of beta-glucosidase A from Paenibacillus polymyxa complexed with multivalent inhibitors.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0008422molecular_functionbeta-glucosidase activity
A0016052biological_processcarbohydrate catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030245biological_processcellulose catabolic process
A0102483molecular_functionscopolin beta-glucosidase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0008422molecular_functionbeta-glucosidase activity
B0016052biological_processcarbohydrate catabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030245biological_processcellulose catabolic process
B0102483molecular_functionscopolin beta-glucosidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue JJW A 501
ChainResidue
AGLN20
AGLU405
ATRP406
AHIS121
ATRP122
AASN165
AGLU166
ALEU173
ATYR296
AGLU352
ATRP398

site_idAC2
Number of Residues11
Detailsbinding site for residue JJW B 501
ChainResidue
BGLN20
BHIS121
BTRP122
BASN165
BGLU166
BLEU173
BGLU352
BTRP398
BGLU405
BTRP406
BHOH622

Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. IYITENGAC
ChainResidueDetails
AILE348-CYS356

site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FmWGtAtAAYQiEgA
ChainResidueDetails
APHE10-ALA24

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255
ChainResidueDetails
AGLU166
BGLU166

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055
ChainResidueDetails
AGLU352
BGLU352

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon