› 3r44

X-ray diffraction
1.8Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162046 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Long-chain-fatty-acid--CoA ligase FadD13 Chain: A
Molecule details ›
Chain: A
Length: 517 amino acids
Theoretical weight: 56.23 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WQ37 (Residues: 1-503; Coverage: 100%)
Gene names: Rv3089, fadD13
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand HIS 1 x HIS
Ligand MLI 1 x MLI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P3121
Unit cell:
a: 57Å b: 57Å c: 249.18Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.164 0.162 0.199
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Emerging drugs and drug targets against tuberculosis.
Lambert et al. (2017)
15 other articles

6 mentions without citation

Structures of Mycobacterium tuberculosis FadD10 protein reveal a new type of adenylate-forming enzyme.
Liu et al. (2013)
5 more