› 6a1p

X-ray diffraction
1.51Å resolution

Mandelate oxidase mutant-Y128F with 5-deazariboflavin mononucleotide and phenylpyruvic acid

Released:
DOI: 10.2210/pdb6a1p/pdb
PDB entry 6a1p coloured by chain, front view.
PDB entry 6a1p coloured by chain, side view.
PDB entry 6a1p coloured by chain, top view.
Source organism: Amycolatopsis orientalis
Primary publication:
The flavin mononucleotide cofactor in α-hydroxyacid oxidases exerts its electrophilic/nucleophilic duality in control of the substrate-oxidation level.
Lyu SY, Lin KH, Yeh HW, Li YS, Huang CM, Wang YL, Shih HW, Hsu NS, Wu CJ, Li TL
OpenAccess logo Acta Crystallogr D Struct Biol 75 918-929 (2019)
PMID: 31588923

Function and Biology Details

Reaction catalysed: 
(S)-4-hydroxymandelate + O(2) = 2-(4-hydroxyphenyl)-2-oxoacetate + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-520510 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxymandelate oxidase Chain: A
Molecule details ›
Chain: A
Length: 377 amino acids
Theoretical weight: 40.03 KDa
Source organism: Amycolatopsis orientalis
Expression system: Escherichia coli
UniProt:
  • Canonical: O52792 (Residues: 1-357; Coverage: 100%)
Gene name: hmo
Sequence domains: FMN-dependent dehydrogenase

Ligands and Environments

3 bound ligands:
Ligand 9O9 1 x 9O9
Ligand MG 1 x MG
Ligand PPY 1 x PPY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13C1
Spacegroup: I422
Unit cell:
a: 137.975Å b: 137.975Å c: 111.068Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.17 0.197
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Structural and chemical trapping of flavin-oxide intermediates reveals substrate-directed reaction multiplicity.
Lin et al. (2020)

1 mention without citation

The flavin mononucleotide cofactor in α-hydroxyacid oxidases exerts its electrophilic/nucleophilic duality in control of the substrate-oxidation level.
Lyu et al. (2019)