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PDBsum entry 3l0h

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protein ligands Protein-protein interface(s) links
Transferase PDB id
3l0h
Jmol
Contents
Protein chain
221 a.a. *
Ligands
GTX ×2
Waters ×386
* Residue conservation analysis
PDB id:
3l0h
Name: Transferase
Title: Crystal structure analysis of w21a mutant of human gsta1-1 i with s-hexylglutathione
Structure: Glutathione s-transferase a1. Chain: a, b. Synonym: gth1, ha subunit 1, gst-epsilon, gsta1-1, gst clas member 1. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsta1. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.13Å     R-factor:   0.174     R-free:   0.233
Authors: S.Fanucchi,I.A.Achilonu,R.J.Adamson,M.A.Fernandes,J.P.Burke,
Key ref: D.Balchin et al. (2010). Stability of the domain interface contributes towards the catalytic function at the H-site of class alpha glutathione transferase A1-1. Biochim Biophys Acta, 1804, 2228-2233. PubMed id: 20833278 DOI: 10.1016/j.bbapap.2010.09.003
Date:
10-Dec-09     Release date:   12-Jan-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P08263  (GSTA1_HUMAN) -  Glutathione S-transferase A1
Seq:
Struc:
222 a.a.
221 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.2.5.1.18  - Glutathione transferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: RX + glutathione = HX + R-S-glutathione
RX
+
glutathione
Bound ligand (Het Group name = GTX)
matches with 76.00% similarity
= HX
+ R-S-glutathione
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   3 terms 
  Biological process     metabolic process   6 terms 
  Biochemical function     transferase activity     2 terms  

 

 
    reference    
 
 
DOI no: 10.1016/j.bbapap.2010.09.003 Biochim Biophys Acta 1804:2228-2233 (2010)
PubMed id: 20833278  
 
 
Stability of the domain interface contributes towards the catalytic function at the H-site of class alpha glutathione transferase A1-1.
D.Balchin, S.Fanucchi, I.Achilonu, R.J.Adamson, J.Burke, M.Fernandes, S.Gildenhuys, H.W.Dirr.
 
  ABSTRACT  
 
No abstract given.