› 6ixm

X-ray diffraction
1.6Å resolution

Crystal structure of the ketone reductase ChKRED20 from the genome of Chryseobacterium sp. CA49 complexed with NAD

Released:
DOI: 10.2210/pdb6ixm/pdb
PDB entry 6ixm coloured by chain, front view.
PDB entry 6ixm coloured by chain, side view.
PDB entry 6ixm coloured by chain, top view.
Source organism: Chryseobacterium sp. CA49
Primary publication:
Structure-guided engineering of ChKRED20 from Chryseobacterium sp. CA49 for asymmetric reduction of aryl ketoesters.
Li TB, Zhao FJ, Liu Z, Jin Y, Liu Y, Pei XQ, Zhang ZG, Wang G, Wu ZL
Enzyme Microb Technol 125 29-36 (2019)
PMID: 30885322

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-197840 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Short-chain dehydrogenase reductase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 249 amino acids
Theoretical weight: 26.26 KDa
Source organism: Chryseobacterium sp. CA49
Expression system: Escherichia coli
UniProt:
  • Canonical: X2D0L0 (Residues: 1-249; Coverage: 100%)
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

1 bound ligand:
Ligand NAD 3 x NAD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL18U1
Spacegroup: P212121
Unit cell:
a: 63.891Å b: 113.98Å c: 131.819Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.164 0.192
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Butyryl/Caproyl-CoA:Acetate CoA-transferase: cloning, expression and characterization of the key enzyme involved in medium-chain fatty acid biosynthesis.
Yang et al. (2021)
2 more

1 mention without citation

Crystal structure of a putative short-chain dehydrogenase/reductase from Paraburkholderia xenovorans.
Davidson et al. (2022)