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PDBsum entry 2xf4

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protein ligands metals links
Hydrolase PDB id
2xf4
Jmol
Contents
Protein chain
210 a.a. *
Ligands
PG4
Metals
_ZN
Waters ×97
* Residue conservation analysis
PDB id:
2xf4
Name: Hydrolase
Title: Crystal structure of salmonella enterica serovar typhimurium ycbl
Structure: Hydroxyacylglutathione hydrolase. Chain: a. Fragment: residues 1-210. Engineered: yes
Source: Salmonella enterica. Organism_taxid: 28901. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.30Å     R-factor:   0.194     R-free:   0.228
Authors: A.Stamp,P.Owen,K.El Omari,C.Nichols,M.Lockyer,H.Lamb,I.Charl A.R.Hawkins,D.K.Stammers
Key ref: A.L.Stamp et al. (2010). Structural and functional characterization of Salmonella enterica serovar Typhimurium YcbL: an unusual Type II glyoxalase. Protein Sci, 19, 1897-1905. PubMed id: 20669241
Date:
20-May-10     Release date:   28-Jul-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
B5CE28  (B5CE28_SALET) -  Hydroxyacylglutathione hydrolase
Seq:
Struc:
215 a.a.
210 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   1 term 
  Biochemical function     hydrolase activity     2 terms  

 

 
Protein Sci 19:1897-1905 (2010)
PubMed id: 20669241  
 
 
Structural and functional characterization of Salmonella enterica serovar Typhimurium YcbL: an unusual Type II glyoxalase.
A.L.Stamp, P.Owen, K.El Omari, C.E.Nichols, M.Lockyer, H.K.Lamb, I.G.Charles, A.R.Hawkins, D.K.Stammers.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21310258 U.Suttisansanee, and J.F.Honek (2011).
Bacterial glyoxalase enzymes.
  Semin Cell Dev Biol, 22, 285-292.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.