› 2oo0

X-ray diffraction
1.9Å resolution

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

Released:
DOI: 10.2210/pdb2oo0/pdb
PDB entry 2oo0 coloured by chain, front view.
PDB entry 2oo0 coloured by chain, side view.
PDB entry 2oo0 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: 471 amino acids
Theoretical weight: 52.33 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


Cofactor: Ligand PLP 2 x PLP
3 bound ligands:
Ligand ACT 3 x ACT
Ligand XAP 2 x XAP
Ligand N2P 2 x N2P
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-2
Spacegroup: C2
Unit cell:
a: 108.018Å b: 87.11Å c: 130.08Å
α: 90° β: 91.02° γ: 90°
R-values:
R R work R free
0.187 0.184 0.213
Expression system: Escherichia coli

Quick links

Citations

5 review citations

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

11 mentions without citation

Polyamine homoeostasis as a drug target in pathogenic protozoa: peculiarities and possibilities.
Birkholtz et al. (2011)
10 more