› 1y9d

X-ray diffraction
2.2Å resolution

Pyruvate Oxidase variant V265A from Lactobacillus plantarum

Released:
DOI: 10.2210/pdb1y9d/pdb
PDB entry 1y9d coloured by chain, front view.
PDB entry 1y9d coloured by chain, side view.
PDB entry 1y9d coloured by chain, top view.
Source organism: Lactiplantibacillus plantarum
Primary publication:
The role of Val-265 for flavin adenine dinucleotide (FAD) binding in pyruvate oxidase: FTIR, kinetic, and crystallographic studies on the enzyme variant V265A.
Wille G, Ritter M, Weiss MS, König S, Mäntele W, Hübner G
Biochemistry 44 5086-94 (2005)
PMID: 15794646

Function and Biology Details

Reaction catalysed: 
Pyruvate + phosphate + O(2) = acetyl phosphate + CO(2) + H(2)O(2)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153340 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate oxidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 603 amino acids
Theoretical weight: 66.18 KDa
Source organism: Lactiplantibacillus plantarum
Expression system: Escherichia coli
UniProt:
  • Canonical: P37063 (Residues: 1-603; Coverage: 100%)
Gene names: lp_3589, pox5
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand TPP 4 x TPP

Cofactor: Ligand FAD 4 x FAD
3 bound ligands:
Ligand MG 4 x MG
Ligand NA 2 x NA
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P21
Unit cell:
a: 94.66Å b: 155.78Å c: 100.75Å
α: 90° β: 92.92° γ: 90°
R-values:
R R work R free
0.181 0.178 0.238
Expression system: Escherichia coli

Quick links

Citations

1 review citation

What's in a covalent bond? On the role and formation of covalently bound flavin cofactors.
Heuts et al. (2009)
4 other articles