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4ZOE

Crystal Structure of beta-glucosidase from Listeria innocua

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008152biological_processmetabolic process
A0008422molecular_functionbeta-glucosidase activity
A0009251biological_processglucan catabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0046872molecular_functionmetal ion binding
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0008152biological_processmetabolic process
B0008422molecular_functionbeta-glucosidase activity
B0009251biological_processglucan catabolic process
B0016787molecular_functionhydrolase activity
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
AASP648
ATHR650
AHOH951
AHOH977
AHOH996
AHOH1152

site_idAC2
Number of Residues10
Detailsbinding site for residue GOL A 802
ChainResidue
ATYR564
AASN566
AHOH910
AHOH917
AHOH1059
BTHR207
BHOH985
AARG143
AGLU214
AASN218

site_idAC3
Number of Residues6
Detailsbinding site for residue MG B 801
ChainResidue
BASP648
BTHR650
BHOH1030
BHOH1036
BHOH1079
BHOH1141

site_idAC4
Number of Residues11
Detailsbinding site for residue GOL B 802
ChainResidue
ATHR207
AHOH1012
BARG143
BGLU214
BASN218
BTYR564
BASN566
BLEU568
BHOH914
BHOH923
BHOH1129

Functional Information from PROSITE/UniProt
site_idPS00775
Number of Residues18
DetailsGLYCOSYL_HYDROL_F3 Glycosyl hydrolases family 3 active site. VLRgEmefdGVLISDwgA
ChainResidueDetails
AVAL256-ALA273

218853

PDB entries from 2024-04-24

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