› 1p3y

X-ray diffraction
2.54Å resolution

MrsD from Bacillus sp. HIL-Y85/54728

Released:
DOI: 10.2210/pdb1p3y/pdb
PDB entry 1p3y coloured by chain, front view.
PDB entry 1p3y coloured by chain, side view.
PDB entry 1p3y coloured by chain, top view.
Source organism: Bacillus sp. HIL-Y85/54728
Primary publication:
Structure of MrsD, an FAD-binding protein of the HFCD family.
Blaesse M, Kupke T, Huber R, Steinbacher S
Acta Crystallogr D Biol Crystallogr 59 1414-21 (2003)
PMID: 12876343

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo dodecamer (preferred)
homo 24-mer
Assembly name:
PDBe Complex ID:
PDB-CPX-193136 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mersacidin decarboxylase Chain: 1
Molecule details ›
Chain: 1
Length: 194 amino acids
Theoretical weight: 21.71 KDa
Source organism: Bacillus sp. HIL-Y85/54728
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9RC23 (Residues: 1-194; Coverage: 100%)
Gene name: mrsD
Sequence domains: Flavoprotein
Structure domains: Flavin prenyltransferase-like

Ligands and Environments

1 bound ligand:
Ligand FAD 1 x FAD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: F432
Unit cell:
a: 191.769Å b: 191.769Å c: 191.769Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.221 0.257
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Bacillus subtilis antibiotics: structures, syntheses and specific functions.
Stein T. (2005)
7 more

3 mentions without citation

Structure and mechanism of lanthipeptide biosynthetic enzymes.
van der Donk et al. (2014)
2 more