› 4ee8

X-ray diffraction
1.93Å resolution

Crystal structure of the Novel Phenazine Prenyltransferase EpzP (wildtype)

Released:
DOI: 10.2210/pdb4ee8/pdb
PDB entry 4ee8 coloured by chain, front view.
PDB entry 4ee8 coloured by chain, side view.
PDB entry 4ee8 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:
  • not assigned
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 Chain: A
Molecule details ›
Chain: A
Length: 304 amino acids
Theoretical weight: 33.41 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 SO4 7 x SO4
Ligand CL 1 x CL
Ligand ACT 1 x ACT
Ligand EPE 1 x EPE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P212121
Unit cell:
a: 60.69Å b: 78.32Å c: 83.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.173 0.198
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)