› 4a95

X-ray diffraction
1.55Å resolution

Plasmodium vivax N-myristoyltransferase with quinoline inhibitor

Released:
DOI: 10.2210/pdb4a95/pdb
PDB entry 4a95 coloured by chain, front view.
PDB entry 4a95 coloured by chain, side view.
PDB entry 4a95 coloured by chain, top view.
Source organism: Plasmodium vivax
Primary publication:
Discovery of Plasmodium vivax N-myristoyltransferase inhibitors: screening, synthesis, and structural characterization of their binding mode.
Goncalves V, Brannigan JA, Whalley D, Ansell KH, Saxty B, Holder AA, Wilkinson AJ, Tate EW, Leatherbarrow RJ
J Med Chem 55 3578-82 (2012)
PMID: 22439843

Function and Biology Details

Reaction catalysed: 
Tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107657 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycylpeptide N-tetradecanoyltransferase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 384 amino acids
Theoretical weight: 44.95 KDa
Source organism: Plasmodium vivax
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A5K1A2 (Residues: 27-410; Coverage: 94%)
Gene name: PVX_085815
Sequence domains:
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand NHW 3 x NHW
4 bound ligands:
Ligand 9MT 3 x 9MT
Ligand CL 3 x CL
Ligand MG 3 x MG
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 57.49Å b: 121.56Å c: 179.01Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.186 0.236
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

Post-translational protein modifications in malaria parasites.
Doerig et al. (2015)
7 more

7 mentions without citation

Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT).
Salah Ud-Din et al. (2016)
6 more