› 5k52

X-ray diffraction
2.4Å resolution

Crystal structures of aldehyde deformylating oxygenase from Limnothrix sp. KNUA012

Released:
DOI: 10.2210/pdb5k52/pdb
PDB entry 5k52 coloured by chain, front view.
PDB entry 5k52 coloured by chain, side view.
PDB entry 5k52 coloured by chain, top view.
Source organism: Limnothrix sp. KNUA012
Primary publication:
Crystal structures of aldehyde deformylating oxygenase from Limnothrix sp. KNUA012 and Oscillatoria sp. KNUA011.
Park AK, Kim IS, Jeon BW, Roh SJ, Ryu MY, Baek HR, Jo SW, Kim YS, Park H, Lee JH, Yoon HS, Kim HW
Biochem Biophys Res Commun 477 395-400 (2016)
PMID: 27329814

Function and Biology Details

Reaction catalysed: 
A long-chain aldehyde + O(2) + 2 NADPH = an alkane + formate + H(2)O + 2 NADP(+)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-103200 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aldehyde decarbonylase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 265 amino acids
Theoretical weight: 29.42 KDa
Source organism: Limnothrix sp. KNUA012
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A193CDY9 (Residues: 1-233; Coverage: 100%)
Sequence domains: Long-chain fatty aldehyde decarbonylase
Structure domains: Ferritin

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: P43
Unit cell:
a: 135.658Å b: 135.658Å c: 71.795Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.21 0.262
Expression system: Escherichia coli

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Citations

1 review citation

Recent advances in the improvement of cyanobacterial enzymes for bioalkane production.
Hayashi et al. (2022)
3 other articles