› 4b14

X-ray diffraction
1.5Å resolution

Plasmodium vivax N-myristoyltransferase with a bound benzofuran inhibitor (compound 26)

Released:
DOI: 10.2210/pdb4b14/pdb
PDB entry 4b14 coloured by chain, front view.
PDB entry 4b14 coloured by chain, side view.
PDB entry 4b14 coloured by chain, top view.
Source organism: Plasmodium vivax
Primary publication:
Design and synthesis of inhibitors of Plasmodium falciparum N-myristoyltransferase, a promising target for antimalarial drug discovery.
Yu Z, Brannigan JA, Moss DK, Brzozowski AM, Wilkinson AJ, Holder AA, Tate EW, Leatherbarrow RJ
J Med Chem 55 8879-90 (2012)
PMID: 23035716

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-500621 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycylpeptide N-tetradecanoyltransferase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 385 amino acids
Theoretical weight: 45.08 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
5 bound ligands:
Ligand DMS 3 x DMS
Ligand 4XB 3 x 4XB
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: DIAMOND BEAMLINE I04-1
Spacegroup: P212121
Unit cell:
a: 57.38Å b: 118.96Å c: 179.13Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.254 0.252 0.302
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

N-Myristoyltransferase as a potential drug target in malaria and leishmaniasis.
Tate et al. (2014)
5 more

6 mentions without citation

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