› 4e0t

X-ray diffraction
2.25Å resolution

Crystal structure of CdpNPT in its unbound state

Released:
DOI: 10.2210/pdb4e0t/pdb
PDB entry 4e0t coloured by chain, front view.
PDB entry 4e0t coloured by chain, side view.
PDB entry 4e0t coloured by chain, top view.
Source organism: Aspergillus fumigatus
Primary publication:
Structure and catalytic mechanism of a cyclic dipeptide prenyltransferase with broad substrate promiscuity.
Schuller JM, Zocher G, Liebhold M, Xie X, Stahl M, Li SM, Stehle T
J Mol Biol 422 87-99 (2012)
PMID: 22683356

Function and Biology Details

Reaction catalysed: 
Preferential release of N-terminal tryptophan.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-112297 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cyclic dipeptide prenyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 428 amino acids
Theoretical weight: 48.76 KDa
Source organism: Aspergillus fumigatus
Expression system: Escherichia coli
UniProt:
  • Canonical: D1D8L6 (Residues: 29-440; Coverage: 94%)
Gene name: cdpNPT
Sequence domains: Tryptophan dimethylallyltransferase

Ligands and Environments

4 bound ligands:
Ligand EDO 19 x EDO
Ligand PEG 1 x PEG
Ligand CL 12 x CL
Ligand NA 4 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P212121
Unit cell:
a: 96.51Å b: 137.02Å c: 172.63Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.166 0.193
Expression system: Escherichia coli

Quick links

Citations

6 review citations

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

2 mentions without citation

Expression, purification, crystallization and crystallographic study of the Aspergillus terreus aromatic prenyltransferase AtaPT.
Gao et al. (2015)
1 more