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PDBsum entry 2w21

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protein ligands links
Transferase PDB id
2w21
Jmol
Contents
Protein chain
246 a.a. *
Ligands
SO4 ×4
Waters ×4
* Residue conservation analysis
PDB id:
2w21
Name: Transferase
Title: Crystal structure of the aminoacid kinase domain of the glutamate 5 kinase of escherichia coli.
Structure: Glutamate 5-kinase. Chain: a. Fragment: amino acid kinase domain, residues 1-259. Synonym: gamma-glutamyl kinase. Engineered: yes. Mutation: yes
Source: Escherichia coli. Organism_taxid: 511693. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
2.95Å     R-factor:   0.209     R-free:   0.259
Authors: I.Perez-Arellano,F.Gil-Ortiz,C.Marco-Marin,J.Cervera, V.Rubio
Key ref: I.Perez-Arellano et al. The structure of glutamate 5 kinase of escherichia coli without substrates. To be published, .
Date:
21-Oct-08     Release date:   17-Nov-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P0A7B5  (PROB_ECOLI) -  Glutamate 5-kinase
Seq:
Struc:
367 a.a.
246 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.2.7.2.11  - Glutamate 5-kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Proline Biosynthesis
      Reaction: ATP + L-glutamate = ADP + L-glutamate 5-phosphate
ATP
+ L-glutamate
= ADP
+ L-glutamate 5-phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     proline biosynthetic process   1 term 
  Biochemical function     glutamate 5-kinase activity     1 term