1sbz

X-ray diffraction
2Å resolution

Crystal Structure of dodecameric FMN-dependent Ubix-like Decarboxylase from Escherichia coli O157:H7

Released:

Function and Biology Details

Reaction catalysed:
Prenyl phosphate + FMNH(2) = prenylated FMNH(2) + phosphate
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
PDBe Complex ID:
PDB-CPX-159653 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable UbiX-like flavin prenyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 197 amino acids
Theoretical weight: 22.01 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli
UniProt:
  • Canonical: P69772 (Residues: 1-197; Coverage: 100%)
Gene names: ECs3593, Z4047, ecdB, pad1
Sequence domains: Flavoprotein
Structure domains: Flavin prenyltransferase-like

Ligands and Environments


Cofactor: Ligand FMN 4 x FMN
No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: R3
Unit cell:
a: 95.372Å b: 95.372Å c: 217.538Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.176 0.216
Expression system: Escherichia coli