Structure of PDB 4zo7 Chain B

Receptor sequence
>4zo7B (length=724) Species: 272626 (Listeria innocua Clip11262) [Search protein sequence]
MEQEKVQELVSQMTLDEKIAQCLQLSPFLFKGTNKNAELTGPLLQEMKLT
DAHTENAGSVLGSSSALDMIGIQEAYLKTNRLGIPLVFMADVIHGYKTVF
PIPLALGCSFDRETVRVMAEVSALEATADGHHVTFSPMLDLVRDPRWGRV
MESTGEDPFLNSELGKAMVDGYQGDASKLNENLEQMAACVKHFAAYGAAE
AGLEYNTVNMSTRELYQNYLPAYNAAIQAGAKLVMTAFNVVDGIPATMNK
WLNRDVLRGEMEFDGVLISAWGAVAEVINHGTARNPKEAAQFSMEAGVDL
EMMTTCYIHELKGLIEEGKLSENLLDEAVLRMLNLKNDLGLFEDPYRGLK
NNDRTKDILTDESRGKARAAGVESAVLLENKSRLLPLAKEAKIALVGPLA
TSPDILGGWNVYGEEKDGINVETGLREVFETVEVVSTEYTELSEEDKVAV
KAAVQNMDVVVLALGEKNEWGGEAGSLATIRLPEAQYQLAKFVQTLGKPV
VITLFNGRPLEVKELAESSDALLELWFPGTEAGRVTADLLSGASNPSGKL
SMSFPQTTGQIPVYYNHLRTGRPQTPENKGERYVSHYLDIPNEPFYPFGY
GKSYSEFELKTSSLPKELNLGESLHVEVTIKNISDIAGKEVIQVYLQDVT
ASISRPVKELKAFEKVALQAGEEKTVTFELTSEAFSFYNHQLEKVQEPGL
HRVFVGTSSEDVDVFEVEVGGYVL
3D structure
PDB4zo7 Functional and Structural Analysis of a beta-Glucosidase Involved in beta-1,2-Glucan Metabolism in Listeria innocua
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A270 G471
Catalytic site (residue number reindexed from 1) A270 G471
Enzyme Commision number 3.2.1.21: beta-glucosidase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 GLC B Y600 E710 D711 Y600 E710 D711
BS02 BGC B E379 F595 E379 F595
BS03 BGC B W271 E473 W271 E473
BS04 MG B D648 T650 D648 T650
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008422 beta-glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009251 glucan catabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4zo7, PDBe:4zo7, PDBj:4zo7
PDBsum4zo7
PubMed26886583
UniProtQ92AS9

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