› 4l4x

X-ray diffraction
2.55Å resolution

An A2-type ketoreductase from a modular polyketide synthase

Released:
DOI: 10.2210/pdb4l4x/pdb
PDB entry 4l4x coloured by chain, front view.
PDB entry 4l4x coloured by chain, side view.
PDB entry 4l4x coloured by chain, top view.
Source organism: Streptomyces nodosus
Primary publication:
Structural studies of an A2-type modular polyketide synthase ketoreductase reveal features controlling α-substituent stereochemistry.
Zheng J, Piasecki SK, Keatinge-Clay AT
ACS Chem Biol 8 1964-71 (2013)
PMID: 23755878

Function and Biology Details

Reaction catalysed: 
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188108 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AmphI Chain: A
Molecule details ›
Chain: A
Length: 580 amino acids
Theoretical weight: 61.33 KDa
Source organism: Streptomyces nodosus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q93NX9 (Residues: 4200-4759; Coverage: 6%)
Gene name: amphI
Sequence domains:
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NDP 1 x NDP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: C2221
Unit cell:
a: 45.139Å b: 133.513Å c: 185.137Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.227 0.28
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

14 review citations

The structural biology of biosynthetic megaenzymes.
Weissman KJ. (2015)
13 more

3 mentions without citation

Stereocontrol within polyketide assembly lines.
Keatinge-Clay AT. (2016)
2 more