› 2ed4

X-ray diffraction
1.85Å resolution

Crystal structure of flavin reductase HpaC complexed with FAD and NAD

Released:
DOI: 10.2210/pdb2ed4/pdb
PDB entry 2ed4 coloured by chain, front view.
PDB entry 2ed4 coloured by chain, side view.
PDB entry 2ed4 coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Crystal structure of the flavin reductase component (HpaC) of 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8: Structural basis for the flavin affinity.
Kim SH, Hisano T, Iwasaki W, Ebihara A, Miki K
Proteins 70 718-30 (2008)
PMID: 17729270

Function and Biology Details

Reaction catalysed: 
Reduced flavin + NAD(+) = flavin + NADH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178031 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxyphenylacetate 3-monooxygenase, reductase component Chains: A, B
Molecule details ›
Chains: A, B
Length: 149 amino acids
Theoretical weight: 16.06 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5SJP7 (Residues: 1-149; Coverage: 100%)
Gene name: TTHA0961
Sequence domains: Flavin reductase like domain
Structure domains: Electron Transport, Fmn-binding Protein; Chain A

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL45XU
Spacegroup: P21
Unit cell:
a: 41.746Å b: 43.655Å c: 74.788Å
α: 90° β: 93.7° γ: 90°
R-values:
R R work R free
0.177 0.177 0.213
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Mechanisms of reduced flavin transfer in the two-component flavin-dependent monooxygenases.
Sucharitakul et al. (2014)
19 other articles

3 mentions without citation

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