› 7odc

X-ray diffraction
1.6Å resolution

CRYSTAL STRUCTURE ORNITHINE DECARBOXYLASE FROM MOUSE, TRUNCATED 37 RESIDUES FROM THE C-TERMINUS, TO 1.6 ANGSTROM RESOLUTION

Released:
DOI: 10.2210/pdb7odc/pdb
PDB entry 7odc coloured by chain, front view.
PDB entry 7odc coloured by chain, side view.
PDB entry 7odc coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structure of mammalian ornithine decarboxylase at 1.6 A resolution: stereochemical implications of PLP-dependent amino acid decarboxylases.
Kern AD, Oliveira MA, Coffino P, Hackert ML
Structure 7 567-81 (1999)
PMID: 10378276

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-133643 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ornithine decarboxylase Chain: A
Molecule details ›
Chain: A
Length: 424 amino acids
Theoretical weight: 47.28 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00860 (Residues: 1-424; Coverage: 92%)
Gene names: Odc, Odc1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 1 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P21212
Unit cell:
a: 118.5Å b: 74Å c: 45.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.199 0.232
Expression system: Escherichia coli

Quick links

Citations

24 review citations

Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations.
Eliot et al. (2004)
23 more

16 mentions without citation

Database of traditional Chinese medicine and its application to studies of mechanism and to prescription validation.
Chen et al. (2006)
15 more