› 2a9g

X-ray diffraction
2.3Å resolution

Structure of C406A arginine deiminase in complex with L-arginine

Released:
DOI: 10.2210/pdb2a9g/pdb
PDB entry 2a9g coloured by chain, front view.
PDB entry 2a9g coloured by chain, side view.
PDB entry 2a9g coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Crystal structures representing the Michaelis complex and the thiouronium reaction intermediate of Pseudomonas aeruginosa arginine deiminase.
Galkin A, Lu X, Dunaway-Mariano D, Herzberg O
J Biol Chem 280 34080-7 (2005)
PMID: 16091358

Function and Biology Details

Reaction catalysed: 
L-arginine + H(2)O = L-citrulline + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domain:
Structure domain:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146825 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arginine deiminase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 418 amino acids
Theoretical weight: 46.46 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: P13981 (Residues: 1-418; Coverage: 100%)
Gene names: PA5171, arcA
Sequence domains: Arginine deiminase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ARG 4 x ARG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 91.1Å b: 120.7Å c: 151Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.199 0.267
Expression system: Escherichia coli

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Citations

5 review citations

Chemical mechanisms of histone lysine and arginine modifications.
Smith et al. (2009)
4 more

7 mentions without citation

Mechanistic similarity and diversity among the guanidine-modifying members of the pentein superfamily.
Linsky et al. (2010)
6 more