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5XXL

Crystal structure of GH3 beta-glucosidase from Bacteroides thetaiotaomicron

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008422molecular_functionbeta-glucosidase activity
A0009251biological_processglucan catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0046872molecular_functionmetal ion binding
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0008422molecular_functionbeta-glucosidase activity
B0009251biological_processglucan catabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MG A 801
ChainResidue
AASP699
AVAL701
AHOH935
AHOH938
AHOH995
AHOH1111

site_idAC2
Number of Residues4
Detailsbinding site for residue PEG A 802
ChainResidue
BTYR593
AARG371
AHOH953
BARG383

site_idAC3
Number of Residues7
Detailsbinding site for residue PG4 A 803
ChainResidue
APHE32
ALEU36
ALYS39
ALEU101
ATHR546
ALYS548
AHOH903

site_idAC4
Number of Residues6
Detailsbinding site for residue MG B 801
ChainResidue
BASP699
BVAL701
BHOH988
BHOH999
BHOH1050
BHOH1076

Functional Information from PROSITE/UniProt
site_idPS00775
Number of Residues18
DetailsGLYCOSYL_HYDROL_F3 Glycosyl hydrolases family 3 active site. VLRgQwgfnGFVVTDytG
ChainResidueDetails
AVAL272-GLY289

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PDB entries from 2024-10-30

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