› 4udr

X-ray diffraction
1.6Å resolution

Crystal structure of the H467A mutant of 5-hydroxymethylfurfural oxidase (HMFO)

Released:
DOI: 10.2210/pdb4udr/pdb
PDB entry 4udr coloured by chain, front view.
PDB entry 4udr coloured by chain, side view.
PDB entry 4udr coloured by chain, top view.
Source organism: Methylovorus sp. MP688
Primary publication:
Structure-Based Enzyme Tailoring of 5-Hydroxymethylfurfural Oxidase
Dijkman WP, Binda C, Fraaije MW, Mattevi A
ACS Catalysis 5 1833- (2015)

Function and Biology Details

Reaction catalysed: 
(1a) 5-(hydroxymethyl)furfural + O(2) = furan-2,5-dicarbaldehyde + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-513875 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
5-(hydroxymethyl)furfural oxidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 531 amino acids
Theoretical weight: 57.01 KDa
Source organism: Methylovorus sp. MP688
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: E4QP00 (Residues: 1-531; Coverage: 100%)
Gene name: MPQ_0130
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
1 bound ligand:
Ligand FMT 2 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 50.82Å b: 122.5Å c: 73.27Å
α: 90° β: 91.12° γ: 90°
R-values:
R R work R free
0.178 0.176 0.218
Expression system: Escherichia coli BL21(DE3)

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