› 1hqg

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF THE H141C ARGINASE VARIANT COMPLEXED WITH PRODUCTS ORNITHINE AND UREA

Released:
DOI: 10.2210/pdb1hqg/pdb
PDB entry 1hqg coloured by chain, front view.
PDB entry 1hqg coloured by chain, side view.
PDB entry 1hqg coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Mechanistic and metabolic inferences from the binding of substrate analogues and products to arginase.
Cox JD, Cama E, Colleluori DM, Pethe S, Boucher JL, Mansuy D, Ash DE, Christianson DW
Biochemistry 40 2689-701 (2001)
PMID: 11258880

Function and Biology Details

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

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: 35.06 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

3 bound ligands:
Ligand MN 6 x MN
Ligand ORN 3 x ORN
Ligand URE 3 x URE
1 modified residue:
Ligand CME 3 x CME

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P32
Unit cell:
a: 88.2Å b: 88.2Å c: 106.5Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.243 0.243 0.232
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Arginase and vascular aging.
Santhanam et al. (2008)
9 more

3 mentions without citation

X-ray Crystallography and Electron Paramagnetic Resonance Spectroscopy Reveal Active Site Rearrangement of Cold-Adapted Inorganic Pyrophosphatase.
Horitani et al. (2020)
2 more