› 1ng4

X-ray diffraction
2.3Å resolution

Structure of ThiO (glycine oxidase) from Bacillus subtilis

Released:
DOI: 10.2210/pdb1ng4/pdb
PDB entry 1ng4 coloured by chain, front view.
PDB entry 1ng4 coloured by chain, side view.
PDB entry 1ng4 coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Structural and mechanistic studies on ThiO, a glycine oxidase essential for thiamin biosynthesis in Bacillus subtilis.
Settembre EC, Dorrestein PC, Park JH, Augustine AM, Begley TP, Ealick SE
Biochemistry 42 2971-81 (2003)
PMID: 12627963

Function and Biology Details

Reaction catalysed: 
(1a) glycine + O(2) = 2-iminoacetate + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128315 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycine oxidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 390 amino acids
Theoretical weight: 43.55 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: O31616 (Residues: 1-369; Coverage: 100%)
Gene names: BSU11670, goxB, thiO, yjbR
Sequence domains: FAD dependent oxidoreductase
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
2 bound ligands:
Ligand PEO 2 x PEO
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 8-BM
Spacegroup: P6122
Unit cell:
a: 139.456Å b: 139.456Å c: 210.278Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.203 0.203 0.234
Expression system: Escherichia coli

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Citations

13 review citations

Radical S-adenosylmethionine enzymes.
Broderick et al. (2014)
12 more

2 mentions without citation

Oxidation of amines by flavoproteins.
Fitzpatrick PF. (2010)
1 more