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PDBsum entry 2d32

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protein ligands metals Protein-protein interface(s) links
Ligase PDB id
2d32
Jmol
Contents
Protein chains
510 a.a. *
Ligands
GLU ×4
CYS ×4
ANP ×4
Metals
_MG ×13
Waters ×800
* Residue conservation analysis
PDB id:
2d32
Name: Ligase
Title: Crystal structure of michaelis complex of gamma- glutamylcysteine synthetase
Structure: Glutamate--cysteine ligase. Chain: a, b, c, d. Synonym: gamma-glutamylcysteine synthetase, gamma-ecs, gcs. Engineered: yes. Mutation: yes
Source: Escherichia coli. Organism_taxid: 562. Gene: gshi. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Tetramer (from PQS)
Resolution:
2.40Å     R-factor:   0.170     R-free:   0.198
Authors: T.Hibi,M.Nakayama,H.Nii,Y.Kurokawa,H.Katano,J.Oda
Key ref: T.Hibi et al. Structural basis of efficient coupling peptide ligation and atp hydrolysis by gamma-Gluatamylcysteine synthetase. To be published, .
Date:
25-Sep-05     Release date:   14-Nov-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P0A6W9  (GSH1_ECOLI) -  Glutamate--cysteine ligase
Seq:
Struc:
518 a.a.
510 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.6.3.2.2  - Glutamate--cysteine ligase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L- cysteine
ATP
+
L-glutamate
Bound ligand (Het Group name = GLU)
corresponds exactly
+
L-cysteine
Bound ligand (Het Group name = CYS)
corresponds exactly
=
ADP
Bound ligand (Het Group name = ANP)
matches with 81.00% similarity
+ phosphate
+ gamma-L-glutamyl-L- cysteine
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     cellular response to arsenic-containing substance   4 terms 
  Biochemical function     nucleotide binding     5 terms