› 4x9n

X-ray diffraction
2.5Å resolution

Dithionite reduced L-alpha-Glycerophosphate Oxidase from Mycoplasma pneumoniae with FAD bound

Released:
DOI: 10.2210/pdb4x9n/pdb
Model geometry
Fit model/data
PDB entry 4x9n coloured by chain, front view.
PDB entry 4x9n coloured by chain, side view.
PDB entry 4x9n coloured by chain, top view.
Source organism: Mycoplasma pneumoniae M129
Primary publication:
Structure and proposed mechanism of L-α-glycerophosphate oxidase from Mycoplasma pneumoniae.
Elkhal CK, Kean KM, Parsonage D, Maenpuen S, Chaiyen P, Claiborne A, Karplus PA
FEBS J 282 3030-42 (2015)
PMID: 25688572

Function and Biology Details

Reaction catalysed: 
sn-glycerol 3-phosphate + O(2) = glycerone phosphate + H(2)O(2)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159966 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycerol 3-phosphate oxidase Chain: A
Molecule details ›
Chain: A
Length: 418 amino acids
Theoretical weight: 46.33 KDa
Source organism: Mycoplasma pneumoniae M129
Expression system: Escherichia coli
UniProt:
  • Canonical: P75063 (Residues: 1-384; Coverage: 100%)
Gene names: D09_orf384, MP103, MPN_051, glpD
Sequence domains: FAD dependent oxidoreductase
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
1 bound ligand:
Ligand NI 1 x NI
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P23
Unit cell:
a: 111.605Å b: 111.605Å c: 111.605Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.15 0.146 0.21
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Insights into the pathogenesis of Mycoplasma pneumoniae (Review).
He et al. (2016)
4 more

1 mention without citation

Structure and proposed mechanism of L-α-glycerophosphate oxidase from Mycoplasma pneumoniae.
Elkhal et al. (2015)