› 7s3f

X-ray diffraction
2.49Å resolution

Structure of cofactor pyridoxal 5-phosphate bound human ornithine decarboxylase in complex with its inhibitor 1-amino-oxy-3-aminopropane

Released:
DOI: 10.2210/pdb7s3f/pdb
PDB entry 7s3f coloured by chain, front view.
PDB entry 7s3f coloured by chain, side view.
PDB entry 7s3f coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of binding and inhibition of ornithine decarboxylase by 1-amino-oxy-3-aminopropane.
Zhou XE, Suino-Powell K, Schultz CR, Aleiwi B, Brunzelle JS, Lamp J, Vega IE, Ellsworth E, Bachmann AS, Melcher K
Biochem J 478 4137-4149 (2021)
PMID: 34796899

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-536663 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ornithine decarboxylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 424 amino acids
Theoretical weight: 47.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11926 (Residues: 1-424; Coverage: 92%)
Gene name: ODC1
Sequence domains:

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P212121
Unit cell:
a: 75.04Å b: 86.9Å c: 154.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.18 0.208
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Biogenic Polyamines and Related Metabolites.
Ivanov et al. (2021)
1 more

1 mention without citation

Structure and Enzymatic Activity of an Intellectual Disability-Associated Ornithine Decarboxylase Variant, G84R.
Zhou et al. (2022)