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PDBsum entry 2xm2

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
2xm2
Jmol
Contents
Protein chains
635 a.a.
Ligands
LOG ×2
GOL ×4
Waters ×775
PDB id:
2xm2
Name: Hydrolase
Title: Btgh84 in complex with lognac
Structure: O-glcnacase bt_4395. Chain: a, b. Synonym: beta-hexosaminidase, n-acetyl-beta-glucosaminidase btgh84, beta-n-acetylhexosaminidase, hexosaminidase b, gh8 engineered: yes
Source: Bacteroides thetaiotaomicron vpi-5482. Organism_taxid: 226186. Atcc: 29148. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
1.95Å     R-factor:   0.182     R-free:   0.220
Authors: Y.He,G.J.Davies
Key ref: Y.He et al. (2011). Inhibition of a bacterial O-GlcNAcase homologue by lactone and lactam derivatives: structural, kinetic and thermodynamic analyses. Amino Acids, 40, 829-839. PubMed id: 20689974
Date:
22-Jul-10     Release date:   03-Aug-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q89ZI2  (OGA_BACTN) -  O-GlcNAcase BT_4395
Seq:
Struc:
 
Seq:
Struc:
737 a.a.
635 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.169  - Protein O-GlcNAcase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. [Protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine + H2O = [protein]- L-serine + N-acetyl-D-glucosamine
2. [Protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine + H2O = [protein]-L-threonine + N-acetyl-D-glucosamine
[Protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine
+ H(2)O
= [protein]- L-serine
+ N-acetyl-D-glucosamine
[Protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine
+ H(2)O
= [protein]-L-threonine
+ N-acetyl-D-glucosamine
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   2 terms 
  Biochemical function     hydrolase activity     2 terms  

 

 
    reference    
 
 
Amino Acids 40:829-839 (2011)
PubMed id: 20689974  
 
 
Inhibition of a bacterial O-GlcNAcase homologue by lactone and lactam derivatives: structural, kinetic and thermodynamic analyses.
Y.He, A.K.Bubb, K.A.Stubbs, T.M.Gloster, G.J.Davies.
 
  ABSTRACT  
 
No abstract given.