› 1c4k

X-ray diffraction
2.7Å resolution

ORNITHINE DECARBOXYLASE MUTANT (GLY121TYR)

Released:
DOI: 10.2210/pdb1c4k/pdb
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Source organism: Lactobacillus sp. 30A
Primary publication:
Three-dimensional structure of the Gly121Tyr dimeric form of ornithine decarboxylase from Lactobacillus 30a.
Vitali J, Carroll D, Chaudhry RG, Hackert ML
Acta Crystallogr D Biol Crystallogr 55 1978-85 (1999)
PMID: 10666573

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-154947 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Inducible ornithine decarboxylase Chain: A
Molecule details ›
Chain: A
Length: 730 amino acids
Theoretical weight: 82.76 KDa
Source organism: Lactobacillus sp. 30A
Expression system: Escherichia coli
UniProt:
  • Canonical: P43099 (Residues: 2-731; Coverage: 100%)
Gene name: odcI
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 1 x PLP
1 bound ligand:
Ligand GTP 1 x GTP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P3221
Unit cell:
a: 111.8Å b: 111.8Å c: 135.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.212 0.212 0.281
Expression system: Escherichia coli

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Citations

7 citation in other articles

Aspartate-107 and leucine-109 facilitate efficient coupling of glutamine hydrolysis to CTP synthesis by Escherichia coli CTP synthase.
Iyengar et al. (2003)
6 more

3 mentions without citation

On the molecular discrimination between adenine and guanine by proteins.
Nobeli et al. (2001)
2 more

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