› 3e6k

X-ray diffraction
2.1Å resolution

X-ray structure of Human Arginase I: the mutant D183A in complex with ABH

Released:
DOI: 10.2210/pdb3e6k/pdb
PDB entry 3e6k coloured by chain, front view.
PDB entry 3e6k coloured by chain, side view.
PDB entry 3e6k coloured by chain, top view.
Source organism: Homo sapiens
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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138410 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arginase-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 322 amino acids
Theoretical weight: 34.74 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 ABH 2 x ABH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: P3
Unit cell:
a: 90.766Å b: 90.766Å c: 69.501Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.164 0.164 0.245
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

2 mentions without citation

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