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4ZOA

Crystal Structure of beta-glucosidase from Listeria innocua in complex with isofagomine

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 Residues9
Detailsbinding site for residue IFM A 801
ChainResidue
ATHR40
AASP91
APHE135
AARG149
ALYS191
AHIS192
AASP270
AGLU473
AHOH1000

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 802
ChainResidue
AASP648
ATHR650
AHOH930
AHOH997
AHOH1003
AHOH1144

site_idAC3
Number of Residues5
Detailsbinding site for residue PEG B 801
ChainResidue
ATRP470
AARG481
AHOH1070
BLEU588
BHOH1178

site_idAC4
Number of Residues9
Detailsbinding site for residue IFM B 802
ChainResidue
BTHR40
BASP91
BPHE135
BARG149
BLYS191
BHIS192
BASP270
BGLU473
BHOH1081

site_idAC5
Number of Residues6
Detailsbinding site for residue MG B 803
ChainResidue
BASP648
BTHR650
BHOH933
BHOH961
BHOH985
BHOH1128

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

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PDB entries from 2024-11-06

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