X-ray diffraction
2.08Å resolution

Insights into Substrate and Metal Binding from the Crystal Structure of Cyanobacterial Aldehyde Deformylating Oxygenase with Substrate Analogs Bound


Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Aldehyde decarbonylase Chain: A
Molecule details ›
Chain: A
Length: 250 amino acids
Theoretical weight: 28.05 KDa
Source organism: Prochlorococcus marinus str. MIT 9313
Expression system: Escherichia coli
  • Canonical: Q7V6D4 (Residues: 1-243; Coverage: 100%)
Gene name: PMT_1231
Sequence domains: Long-chain fatty aldehyde decarbonylase
Structure domains: Ferritin

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P43212
Unit cell:
a: 77.071Å b: 77.071Å c: 117.259Å
α: 90° β: 90° γ: 90°
R R work R free
0.196 0.194 0.222
Expression system: Escherichia coli