› 2on3

X-ray diffraction
3Å resolution

A structural insight into the inhibition of human and Leishmania donovani ornithine decarboxylases by 3-aminooxy-1-aminopropane

Released:
DOI: 10.2210/pdb2on3/pdb
PDB entry 2on3 coloured by chain, front view.
PDB entry 2on3 coloured by chain, side view.
PDB entry 2on3 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A structural insight into the inhibition of human and Leishmania donovani ornithine decarboxylases by 1-amino-oxy-3-aminopropane.
Dufe VT, Ingner D, Heby O, Khomutov AR, Persson L, Al-Karadaghi S
Biochem J 405 261-8 (2007)
PMID: 17407445

Function and Biology Details

Reaction catalysed: 
L-ornithine = putrescine + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145984 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ornithine decarboxylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 461 amino acids
Theoretical weight: 51.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11926 (Residues: 1-461; Coverage: 100%)
Gene name: ODC1
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand XAP 2 x XAP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-2
Spacegroup: P212121
Unit cell:
a: 60.54Å b: 104.84Å c: 137.35Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.23 0.293
Expression system: Escherichia coli

Quick links

Citations

6 review citations

L-arginine metabolism and its impact on host immunity against Leishmania infection.
Wanasen et al. (2008)
5 more

8 mentions without citation

Structural basis of Ornithine Decarboxylase inactivation and accelerated degradation by polyamine sensor Antizyme1.
Wu et al. (2015)
7 more