› 4dc0

X-ray diffraction
2.81Å resolution

Crystal Structure of F189W Actinorhodin Polyketide Ketoreductase with NADPH

Released:
DOI: 10.2210/pdb4dc0/pdb
PDB 4dc0 coloured by chain and viewed from the front.
PDB 4dc0 coloured by chain and viewed from the side.
PDB 4dc0 coloured by chain and viewed from the top.
Source organism: Streptomyces coelicolor
Primary publication:
The Determinants of Activity and Specificity in Actinorhodin Type II Polyketide Ketoreductase.
Javidpour P, Bruegger J, Srithahan S, Korman TP, Crump MP, Crosby J, Burkart MD, Tsai SC
Chem. Biol. 20 1225-34 (2013)
PMID: 24035284

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative ketoacyl reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 281 amino acids
Theoretical weight: 29.5 KDa
Source organism: Streptomyces coelicolor
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P16544 (Residues: 1-261; Coverage: 100%)
Gene names: SCBAC28G1.12c, SCO5086, actIII
Sequence domains: short chain dehydrogenase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P3221
Unit cell:
a: 103.527Å b: 103.527Å c: 123.232Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.191 0.188 0.246
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

The Structural Enzymology of Iterative Aromatic Polyketide Synthases: A Critical Comparison with Fatty Acid Synthases.
Tsai SC. (2018)
1 more

1 mention without citation

The determinants of activity and specificity in actinorhodin type II polyketide ketoreductase.
Javidpour et al. (2013)