› 4ee7

X-ray diffraction
1.67Å resolution

Crystal Structure of the Novel Phenazine Prenyltransferase EpzP in complex with S-thiolodiphosphate (methylated)

Released:
DOI: 10.2210/pdb4ee7/pdb
PDB entry 4ee7 coloured by chain, front view.
PDB entry 4ee7 coloured by chain, side view.
PDB entry 4ee7 coloured by chain, top view.
Source organism: Streptomyces virginiae
Primary publication:
Structure-based engineering increased the catalytic turnover rate of a novel phenazine prenyltransferase.
Zocher G, Saleh O, Heim JB, Herbst DA, Heide L, Stehle T
PLoS One 7 e48427 (2012)
PMID: 23119011

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-122984 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prenyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 304 amino acids
Theoretical weight: 33.55 KDa
Source organism: Streptomyces virginiae
Expression system: Escherichia coli
UniProt:
  • Canonical: E5KWG9 (Residues: 1-302; Coverage: 100%)
Gene name: epzP
Sequence domains: Aromatic prenyltransferase Orf2

Ligands and Environments

4 bound ligands:
Ligand PIS 1 x PIS
Ligand PG4 4 x PG4
Ligand SO4 6 x SO4
Ligand CL 1 x CL
1 modified residue:
Ligand MLY 10 x MLY

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P212121
Unit cell:
a: 42.11Å b: 97.01Å c: 135.86Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.188 0.224
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Prenyltransferases as key enzymes in primary and secondary metabolism.
Winkelblech et al. (2015)
4 more

1 mention without citation

Structure-based engineering increased the catalytic turnover rate of a novel phenazine prenyltransferase.
Zocher et al. (2012)