4xgw

X-ray diffraction
1.75Å resolution

Crystal structure of Escherichia coli Flavin trafficking protein, an FMN transferase, E169K mutant

Released:

Function and Biology Details

Reaction catalysed:
FAD + [protein]-L-threonine = [protein]-FMN-L-threonine + AMP
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-142024 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FAD:protein FMN transferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 340 amino acids
Theoretical weight: 37.65 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AB85 (Residues: 21-351; Coverage: 100%)
Gene names: JW5368, apbE, b2214, yojK, yojL
Sequence domains: ApbE family
Structure domains: ApbE-like domains

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P1
Unit cell:
a: 57.216Å b: 70.65Å c: 86.276Å
α: 75.72° β: 71.91° γ: 69.72°
R-values:
R R work R free
0.173 0.172 0.198
Expression system: Escherichia coli BL21(DE3)