› 1lxy

X-ray diffraction
2Å resolution

Crystal Structure of Arginine Deiminase covalently linked with L-citrulline

Released:
DOI: 10.2210/pdb1lxy/pdb
PDB entry 1lxy coloured by chain, front view.
PDB entry 1lxy coloured by chain, side view.
PDB entry 1lxy coloured by chain, top view.
Source organism: Mycoplasmopsis arginini
Primary publication:
Crystal structures of arginine deiminase with covalent reaction intermediates; implications for catalytic mechanism.
Das K, Butler GH, Kwiatkowski V, Clark AD, Yadav P, Arnold E
Structure 12 657-67 (2004)
PMID: 15062088

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

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150060 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arginine deiminase Chains: A, B
Molecule details ›
Chains: A, B
Length: 409 amino acids
Theoretical weight: 46.43 KDa
Source organism: Mycoplasmopsis arginini
UniProt:
  • Canonical: P23793 (Residues: 2-410; Coverage: 100%)
Gene name: arcA
Sequence domains: Arginine deiminase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CIR 2 x CIR
Ligand TRS 2 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21
Unit cell:
a: 77.24Å b: 76.37Å c: 82.9Å
α: 90° β: 109.74° γ: 90°
R-values:
R R work R free
0.186 0.186 0.227

Quick links

Citations

11 review citations

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

3 mentions without citation

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