› 2d37

X-ray diffraction
1.7Å resolution

The Crystal Structure of Flavin Reductase HpaC complexed with NAD+

Released:
DOI: 10.2210/pdb2d37/pdb
PDB entry 2d37 coloured by chain, front view.
PDB entry 2d37 coloured by chain, side view.
PDB entry 2d37 coloured by chain, top view.
Source organism: Sulfurisphaera tokodaii str. 7
Primary publication:
Crystal structures of the short-chain flavin reductase HpaC from Sulfolobus tokodaii strain 7 in its three states: NAD(P)(+)(-)free, NAD(+)(-)bound, and NADP(+)(-)bound.
Okai M, Kudo N, Lee WC, Kamo M, Nagata K, Tanokura M
Biochemistry 45 5103-10 (2006)
PMID: 16618099

Function and Biology Details

Reaction catalysed: 
Phenol + NADPH + O(2) = catechol + NADP(+) + H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188834 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Flavin reductase like domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 176 amino acids
Theoretical weight: 20.16 KDa
Source organism: Sulfurisphaera tokodaii str. 7
Expression system: Escherichia coli
UniProt:
  • Canonical: Q974C9 (Residues: 1-156; Coverage: 100%)
Gene names: ST0723, STK_07230, pheA2
Sequence domains: Flavin reductase like domain
Structure domains: Electron Transport, Fmn-binding Protein; Chain A

Ligands and Environments


Cofactor: Ligand NAD 1 x NAD
1 bound ligand:
Ligand FMN 1 x FMN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P3121
Unit cell:
a: 86.449Å b: 86.449Å c: 49.029Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.179 0.179 0.2
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Monooxygenation of aromatic compounds by flavin-dependent monooxygenases.
Chenprakhon et al. (2019)
15 other articles

6 mentions without citation

Two-Component FAD-Dependent Monooxygenases: Current Knowledge and Biotechnological Opportunities.
Heine et al. (2018)
5 more