› 3zoe

X-ray diffraction
1.85Å resolution

Crystal structure of FMN-binding protein (YP_005476) from Thermus thermophilus with bound p-hydroxybenzaldehyde

Released:
DOI: 10.2210/pdb3zoe/pdb
PDB 3zoe coloured by chain and viewed from the front.
PDB 3zoe coloured by chain and viewed from the side.
PDB 3zoe coloured by chain and viewed from the top.
Source organism: Thermus thermophilus HB27
Primary publication:
Identification of promiscuous ene-reductase activity by mining structural databases using active site constellations.
Steinkellner G, Gruber CC, Pavkov-Keller T, Binter A, Steiner K, Winkler C, Lyskowski A, Schwamberger O, Oberer M, Schwab H, Faber K, Macheroux P, Gruber K
Nat Commun 5 4150 (2014)
PMID: 24954722

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Flavin_Reduct domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 178 amino acids
Theoretical weight: 19.74 KDa
Source organism: Thermus thermophilus HB27
Expression system: Escherichia coli
UniProt:
  • Canonical: Q72HI0 (Residues: 1-178; Coverage: 100%)
Gene name: TT_C1507
Sequence domains: Flavin reductase like domain
Structure domains: Electron Transport, Fmn-binding Protein; Chain A

Ligands and Environments

2 bound ligands:
Ligand HBA 2 x HBA
Ligand FMN 2 x FMN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P212121
Unit cell:
a: 64.66Å b: 74.91Å c: 77.59Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.244 0.242 0.278
Expression system: Escherichia coli

Quick links

Citations

4 review citations

How enzyme promiscuity and horizontal gene transfer contribute to metabolic innovation.
Glasner et al. (2020)
3 more

2 mentions without citation

Identification of promiscuous ene-reductase activity by mining structural databases using active site constellations.
Steinkellner et al. (2014)
1 more