› 4fci

X-ray diffraction
1.82Å resolution

Crystal Structure of the Mn2+2-Human Arginase I-AGPA Complex

Released:
DOI: 10.2210/pdb4fci/pdb
PDB entry 4fci coloured by chain, front view.
PDB entry 4fci coloured by chain, side view.
PDB entry 4fci coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Binding of the unreactive substrate analog L-2-amino-3-guanidinopropionic acid (dinor-L-arginine) to human arginase I.
D'Antonio EL, Christianson DW
Acta Crystallogr Sect F Struct Biol Cryst Commun 68 889-93 (2012)
PMID: 22869115

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 GPA 1 x GPA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P3
Unit cell:
a: 90.848Å b: 90.848Å c: 69.767Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.278 0.278 0.31
Expression system: Escherichia coli

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Citations

2 mentions 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)
1 more