1t5f

X-ray diffraction
2.2Å resolution

arginase I-AOH complex

Released:
Source organism: Rattus norvegicus
Primary publication:
Design of amino acid aldehydes as transition-state analogue inhibitors of arginase.
J. Am. Chem. Soc. 126 10278-84 (2004)
PMID: 15315440

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arginase-1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 314 amino acids
Theoretical weight: 33.85 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P07824 (Residues: 6-319; Coverage: 97%)
Gene name: Arg1
Structure domains: Ureohydrolase domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P32
Unit cell:
a: 87.9Å b: 87.9Å c: 105.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.222 0.222 0.241
Expression system: Escherichia coli