› 5y72

X-ray diffraction
1.65Å resolution

DMSPP Bound AmbP3

Released:
DOI: 10.2210/pdb5y72/pdb
PDB entry 5y72 coloured by chain, front view.
PDB entry 5y72 coloured by chain, side view.
PDB entry 5y72 coloured by chain, top view.
Source organism: Fischerella ambigua UTEX 1903
Primary publication:
Two Distinct Substrate Binding Modes for the Normal and Reverse Prenylation of Hapalindoles by the Prenyltransferase AmbP3.
Wong CP, Awakawa T, Nakashima Y, Mori T, Zhu Q, Liu X, Abe I
Angew Chem Int Ed Engl 57 560-563 (2018)
PMID: 29178634

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-197625 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxyphenylpyruvate 3-dimethylallyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 335 amino acids
Theoretical weight: 38.04 KDa
Source organism: Fischerella ambigua UTEX 1903
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: V5TDY7 (Residues: 1-322; Coverage: 100%)
Gene name: ambP3
Sequence domains: Aromatic prenyltransferase Orf2

Ligands and Environments

1 bound ligand:
Ligand DST 2 x DST
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-1A
Spacegroup: P1
Unit cell:
a: 46.394Å b: 55.08Å c: 77.668Å
α: 105.41° β: 106.02° γ: 98.79°
R-values:
R R work R free
0.182 0.181 0.203
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Quick links

Citations

4 review citations

Structure, catalysis, and inhibition mechanism of prenyltransferase.
Chang et al. (2021)
3 more