› 4rc8

X-ray diffraction
1.71Å resolution

Crystal structure of cyanobacterial aldehyde-deformylating oxygenase bound with fatty acid

Released:
DOI: 10.2210/pdb4rc8/pdb
PDB entry 4rc8 coloured by chain, front view.
PDB entry 4rc8 coloured by chain, side view.
PDB entry 4rc8 coloured by chain, top view.
Source organism: Synechococcus elongatus PCC 7942 = FACHB-805
Primary publication:
Structural insights into the catalytic mechanism of aldehyde-deformylating oxygenases.
Jia C, Li M, Li J, Zhang J, Zhang H, Cao P, Pan X, Lu X, Chang W
Protein Cell 6 55-67 (2015)
PMID: 25482408

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-176220 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aldehyde decarbonylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 222 amino acids
Theoretical weight: 25.4 KDa
Source organism: Synechococcus elongatus PCC 7942 = FACHB-805
Expression system: Escherichia coli
UniProt:
  • Canonical: Q54764 (Residues: 10-231; Coverage: 96%)
Gene name: Synpcc7942_1593
Sequence domains: Long-chain fatty aldehyde decarbonylase
Structure domains: Ferritin

Ligands and Environments

2 bound ligands:
Ligand STE 1 x STE
Ligand FE 2 x FE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P212121
Unit cell:
a: 61.628Å b: 61.984Å c: 124.781Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 0.212
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes.
Jasniewski et al. (2018)
7 more

3 mentions without citation

Structural insights into the functional diversity of the CDK-cyclin family.
Wood et al. (2018)
2 more