PDBsum entry: 2oyk

Hydrolase

PDB id: 2oyk

Contents

Protein chains

434 a.a. *

Ligands

9MR ×2

GOL

Metals

_NA ×4

Waters ×962

* Residue conservation analysis

PDB id:

2oyk

Name:

Hydrolase

Title:

Endo-glycoceramidase ii from rhodococcus sp.: Cellobiose-lik isofagomine complex

Structure:

Endoglycoceramidase ii. Chain: a, b. Engineered: yes

Source:

Rhodococcus sp.. Organism_taxid: 1831. Strain: m-777. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.50Å R-factor: 0.178 R-free: 0.198

Authors:

M.E.C.Caines,N.C.J.Strynadka

Key ref:

M.E.Caines et al. (2007). The structural basis of glycosidase inhibition by five-membered iminocyclitols: the clan a glycoside hydrolase endoglycoceramidase as a model system. Angew Chem Int Ed Engl, 46, 4474-4476. PubMed id: 17487923 DOI: 10.1002/anie.200700268

Date:

22-Feb-07 Release date: 06-Mar-07

Protein chains

O33853  (O33853_RHOSO) -  Endoglycoceramidase II

Seq: 490 a.a.

Struc: 434 a.a.

Enzyme reactions

• Enzyme class: E.C.3.2.1.123 - Endoglycosylceramidase.
• Reaction: Oligoglycosylglucosyl-(1<->1)-ceramide + H₂O = ceramide + oligoglycosylglucose

Oligoglycosylglucosyl-(1<->1)-ceramide + H(2)O = ceramide + oligoglycosylglucose (Bound ligand (Het Group name = 9MR) matches with 54.55% similarity)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Biological process: metabolic process (2 terms)
• Biochemical function: catalytic activity (6 terms)

Added reference

DOI no: 10.1002/anie.200700268

Angew Chem Int Ed Engl 46:4474-4476 (2007)

PubMed id: 17487923

The structural basis of glycosidase inhibition by five-membered iminocyclitols: the clan a glycoside hydrolase endoglycoceramidase as a model system.

M.E.Caines, S.M.Hancock, C.A.Tarling, T.M.Wrodnigg, R.V.Stick, A.E.Stütz, A.Vasella, S.G.Withers, N.C.Strynadka.

ABSTRACT

No abstract given.