› 4fxu

X-ray diffraction
1.9Å resolution

Crystallographic structure of trimeric riboflavin synthase from Brucella abortus

Released:
DOI: 10.2210/pdb4fxu/pdb
PDB entry 4fxu coloured by chain, front view.
PDB entry 4fxu coloured by chain, side view.
PDB entry 4fxu coloured by chain, top view.
Source organism: Brucella abortus
Primary publication:
Crystallographic and kinetic study of riboflavin synthase from Brucella abortus, a chemotherapeutic target with an enhanced intrinsic flexibility.
Serer MI, Bonomi HR, Guimarães BG, Rossi RC, Goldbaum FA, Klinke S
Acta Crystallogr D Biol Crystallogr 70 1419-34 (2014)
PMID: 24816110

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-164477 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Riboflavin synthase subunit alpha Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 210 amino acids
Theoretical weight: 23.32 KDa
Source organism: Brucella abortus
Expression system: Escherichia coli BL21(DE3)
Structure domains: Elongation Factor Tu (Ef-tu); domain 3

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P212121
Unit cell:
a: 67.42Å b: 93.48Å c: 103.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.232 0.264
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Inhibitors of riboflavin biosynthetic pathway enzymes as potential antibacterial drugs.
Islam et al. (2023)
2 other articles

1 mention without citation

Crystallographic and kinetic study of riboflavin synthase from Brucella abortus, a chemotherapeutic target with an enhanced intrinsic flexibility.
Serer et al. (2014)