› 1njj

X-ray diffraction
2.45Å resolution

Crystal structure determination of T. brucei ornithine decarboxylase bound to D-ornithine and to G418

Released:
DOI: 10.2210/pdb1njj/pdb
PDB entry 1njj coloured by chain, front view.
PDB entry 1njj coloured by chain, side view.
PDB entry 1njj coloured by chain, top view.
Source organism: Trypanosoma brucei gambiense
Primary publication:
X-ray structure determination of Trypanosoma brucei ornithine decarboxylase bound to D-ornithine and to G418: insights into substrate binding and ODC conformational flexibility.
Jackson LK, Goldsmith EJ, Phillips MA
J Biol Chem 278 22037-43 (2003)
PMID: 12672797

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193591 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ornithine decarboxylase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 425 amino acids
Theoretical weight: 47.15 KDa
Source organism: Trypanosoma brucei gambiense
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9TZZ6 (Residues: 21-445; Coverage: 96%)
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand GET 3 x GET
Ligand ORX 4 x ORX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 67.818Å b: 88.54Å c: 150.445Å
α: 90° β: 90.03° γ: 90°
R-values:
R R work R free
0.26 0.26 0.283
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

Nutritional and medicinal aspects of D-amino acids.
Friedman et al. (2012)
1 more

9 mentions without citation

A Supramolecular Approach to Structure-Based Design with A Focus on Synthons Hierarchy in Ornithine-Derived Ligands: Review, Synthesis, Experimental and in Silico Studies.
Bojarska et al. (2020)
8 more