› 3lp7

X-ray diffraction
2.04Å resolution

Crystal structure of Human Arginase I in complex with inhibitor N(omega)-hydroxy-L-arginine (NOHA), 2.04A Resolution

Released:
DOI: 10.2210/pdb3lp7/pdb
PDB entry 3lp7 coloured by chain, front view.
PDB entry 3lp7 coloured by chain, side view.
PDB entry 3lp7 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Inhibition of human arginase I by substrate and product analogues.
Di Costanzo L, Ilies M, Thorn KJ, Christianson DW
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:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138411 (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:
Ligand MN 4 x MN
Ligand HAR 2 x HAR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P3
Unit cell:
a: 90.68Å b: 90.68Å c: 69.82Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.123 0.123 0.174
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Nitric oxide and redox mechanisms in the immune response.
Wink et al. (2011)
7 more

3 mentions without citation

Inhibition of human arginase I by substrate and product analogues.
Di Costanzo et al. (2010)
2 more