X-ray diffraction
1.8Å resolution

The Structure of Trp Repressor Binding Protein from Bacillus subtilis

Source organism: Bacillus subtilis
Entry authors: Kim Y, Quartey P, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Putative NAD(P)H-dependent FMN-containing oxidoreductase YwqN Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 184 amino acids
Theoretical weight: 20.78 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
  • Canonical: P96726 (Residues: 1-181; Coverage: 100%)
Gene names: BSU36150, ywqN
Sequence domains: NADPH-dependent FMN reductase
Structure domains: Rossmann fold

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 60.993Å b: 90.666Å c: 63.446Å
α: 90° β: 97.02° γ: 90°
R R work R free
0.199 0.196 0.23
Expression system: Escherichia coli