› 3e8z

X-ray diffraction
2Å resolution

X-ray structure of rat arginase I-N130A mutant: the unliganded complex

Released:
DOI: 10.2210/pdb3e8z/pdb
PDB entry 3e8z coloured by chain, front view.
PDB entry 3e8z coloured by chain, side view.
PDB entry 3e8z coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Probing the specificity determinants of amino acid recognition by arginase.
Shishova EY, Di Costanzo L, Emig FA, Ash DE, Christianson DW
Biochemistry 48 121-31 (2009)
PMID: 19093830

Function and Biology Details

Reaction catalysed: 
L-arginine + H(2)O = L-ornithine + urea
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139779 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arginase-1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 323 amino acids
Theoretical weight: 34.98 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P07824 (Residues: 1-323; Coverage: 100%)
Gene name: Arg1
Sequence domains: Arginase family
Structure domains: Ureohydrolase domain

Ligands and Environments

1 bound ligand:
Ligand MN 6 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F2
Spacegroup: P32
Unit cell:
a: 87.5Å b: 87.5Å c: 100.11Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.236 0.236 0.28
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Manganese and its role in Parkinson's disease: from transport to neuropathology.
Aschner et al. (2009)
2 more

1 mention without citation

Probing the specificity determinants of amino acid recognition by arginase.
Shishova et al. (2009)