› 4ie3

X-ray diffraction
2.35Å resolution

Crystal structure of human Arginase-2 complexed with inhbitor 1o

Released:
DOI: 10.2210/pdb4ie3/pdb
PDB entry 4ie3 coloured by chain, front view.
PDB entry 4ie3 coloured by chain, side view.
PDB entry 4ie3 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
2-Substituted-2-amino-6-boronohexanoic acids as arginase inhibitors.
Golebiowski A, Paul Beckett R, Van Zandt M, Ji MK, Whitehouse D, Ryder TR, Jagdmann E, Andreoli M, Mazur A, Padmanilayam M, Cousido-Siah A, Mitschler A, Ruiz FX, Podjarny A, Schroeter H
Bioorg Med Chem Lett 23 2027-30 (2013)
PMID: 23453840

Function and Biology Details

Reaction catalysed: 
L-arginine + H(2)O = L-ornithine + urea
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo trimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160276 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arginase-2, mitochondrial Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 306 amino acids
Theoretical weight: 33.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P78540 (Residues: 24-329; Coverage: 86%)
Gene name: ARG2
Sequence domains: Arginase family
Structure domains: Ureohydrolase domain

Ligands and Environments

4 bound ligands:
Ligand MN 6 x MN
Ligand BEN 3 x BEN
Ligand BME 4 x BME
Ligand 1EE 3 x 1EE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P42212
Unit cell:
a: 128.086Å b: 128.086Å c: 159.079Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.149 0.146 0.194
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Arginase Inhibitors: A Rational Approach Over One Century.
Pudlo et al. (2017)
3 more

1 mention without citation

Insights into the Structural Requirements of 2(S)-Amino-6-Boronohexanoic Acid Derivatives as Arginase I Inhibitors: 3D-QSAR, Docking, and Interaction Fingerprint Studies.
Velázquez-Libera et al. (2018)