PDBe 3kv2

X-ray diffraction
1.55Å resolution

HIGH RESOLUTION STRUCTURE OF HUMAN ARGINASE I IN COMPLEX WITH THE STRONG INHIBITOR N(omega)-hydroxy-nor-L-arginine (nor-NOHA)

Released:
Source organism: Homo sapiens
Primary publication:
Inhibition of human arginase I by substrate and product analogues.
Arch. Biochem. Biophys. 496 101-8 (2010)
PMID: 20153713

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arginase-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 322 amino acids
Theoretical weight: 34.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05089 (Residues: 1-322; Coverage: 100%)
Gene name: ARG1
Sequence domains: Arginase family
Structure domains: Ureohydrolase domain

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P3
Unit cell:
a: 90.497Å b: 90.497Å c: 69.604Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.144 0.144 0.178
Expression system: Escherichia coli