› 5ygk

X-ray diffraction
2.05Å resolution

Crystal structure of a synthase from Streptomyces sp. CL190 with dmaspp

Released:
DOI: 10.2210/pdb5ygk/pdb
PDB 5ygk coloured by chain and viewed from the front.
PDB 5ygk coloured by chain and viewed from the side.
PDB 5ygk coloured by chain and viewed from the top.
Source organism: Streptomyces sp. CL190
Entry authors: Gao J, Liu WD, Chen CC, Guo RT

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cyclolavandulyl diphosphate synthase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 217 amino acids
Theoretical weight: 24.38 KDa
Source organism: Streptomyces sp. CL190
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: X5IYJ5 (Residues: 1-217; Coverage: 100%)
Sequence domains: Putative undecaprenyl diphosphate synthase

Ligands and Environments

2 bound ligands:
Ligand DST 16 x DST
Ligand MG 8 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE TPS 05A
Spacegroup: P21
Unit cell:
a: 90.09Å b: 119.308Å c: 93.133Å
α: 90° β: 117.35° γ: 90°
R-values:
R R work R free
0.185 0.184 0.236
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Isoprenyl diphosphate synthases: the chain length determining step in terpene biosynthesis.
Nagel et al. (2019)
5 other articles