› 6nkm

X-ray diffraction
1.9Å resolution

Structure of PhqE D166N Reductase/Diels-Alderase from Penicillium fellutanum in complex with NADP+ and substrate

Released:
DOI: 10.2210/pdb6nkm/pdb
PDB entry 6nkm coloured by chain, front view.
PDB entry 6nkm coloured by chain, side view.
PDB entry 6nkm coloured by chain, top view.
Source organism: Penicillium fellutanum
Primary publication:
Fungal indole alkaloid biogenesis through evolution of a bifunctional reductase/Diels-Alderase.
Dan Q, Newmister SA, Klas KR, Fraley AE, McAfoos TJ, Somoza AD, Sunderhaus JD, Ye Y, Shende VV, Yu F, Sanders JN, Brown WC, Zhao L, Paton RS, Houk KN, Smith JL, Sherman DH, Williams RM
Nat Chem 11 972-980 (2019)
PMID: 31548667

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125739 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Short-chain dehydrogenase/reductase phqE Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 265 amino acids
Theoretical weight: 27.55 KDa
Source organism: Penicillium fellutanum
Expression system: Escherichia coli
UniProt:
  • Canonical: L0E2Z4 (Residues: 1-265; Coverage: 100%)
Gene name: phqE
Sequence domains: Enoyl-(Acyl carrier protein) reductase

Ligands and Environments

2 bound ligands:
Ligand NAP 6 x NAP
Ligand ZWP 1 x ZWP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: C2
Unit cell:
a: 209.484Å b: 117.194Å c: 63.731Å
α: 90° β: 107.44° γ: 90°
R-values:
R R work R free
0.276 0.274 0.306
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Repurposing Modular Polyketide Synthases and Non-ribosomal Peptide Synthetases for Novel Chemical Biosynthesis.
Hwang et al. (2020)
3 more

1 mention without citation

Fungal indole alkaloid biogenesis through evolution of a bifunctional reductase/Diels-Alderase.
Dan et al. (2019)