› 6ecv

X-ray diffraction
1.8Å resolution

StiD O-MT residues 976-1266

Released:
DOI: 10.2210/pdb6ecv/pdb
PDB 6ecv coloured by chain and viewed from the front.
PDB 6ecv coloured by chain and viewed from the side.
PDB 6ecv coloured by chain and viewed from the top.
Source organism: Stigmatella aurantiaca
Primary publication:
Structural Basis of Polyketide Synthase O-Methylation.
Skiba MA, Bivins MM, Schultz JR, Bernard SM, Fiers WD, Dan Q, Kulkarni S, Wipf P, Gerwick WH, Sherman DH, Aldrich CC, Smith JL
ACS Chem Biol 13 3221-3228 (2018)
PMID: 30489068

Function and Biology Details

Biochemical function:
  • not assigned
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:
Carrier domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 316 amino acids
Theoretical weight: 35.54 KDa
Source organism: Stigmatella aurantiaca
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8RJY3 (Residues: 976-1267; Coverage: 15%)
Gene name: stiD
Sequence domains: Methyltransferase domain

Ligands and Environments

2 bound ligands:
Ligand SAH 2 x SAH
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P1
Unit cell:
a: 40.182Å b: 56.175Å c: 72.251Å
α: 86.31° β: 84.89° γ: 75.81°
R-values:
R R work R free
0.168 0.167 0.194
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 citations in other articles

General chemoenzymatic route to two-stereocenter triketides employing assembly line ketoreductases.
Zhang et al. (2019)

1 mention without citation

Structural Basis of Polyketide Synthase O-Methylation.
Skiba et al. (2018)