Structure of PDB 4zo9 Chain A

Receptor sequence
>4zo9A (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
PDB4zo9 Functional and Structural Analysis of a beta-Glucosidase Involved in beta-1,2-Glucan Metabolism in Listeria innocua
ChainA
Resolution1.99 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
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
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Biological Process
External links
PDB RCSB:4zo9, PDBe:4zo9, PDBj:4zo9
PDBsum4zo9
PubMed26886583
UniProtQ92AS9

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