› 4c7h

X-ray diffraction
1.4Å resolution

Leismania major N-myristoyltransferase in complex with a peptidomimetic (-NH2) molecule

Released:
DOI: 10.2210/pdb4c7h/pdb
PDB entry 4c7h coloured by chain, front view.
PDB entry 4c7h coloured by chain, side view.
PDB entry 4c7h coloured by chain, top view.
Source organism: Leishmania major
Primary publication:
Peptidomimetic inhibitors of N-myristoyltransferase from human malaria and leishmaniasis parasites.
Olaleye TO, Brannigan JA, Roberts SM, Leatherbarrow RJ, Wilkinson AJ, Tate EW
OpenAccess logo Org Biomol Chem 12 8132-7 (2014)
PMID: 25230674

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-175678 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycylpeptide N-tetradecanoyltransferase Chain: A
Molecule details ›
Chain: A
Length: 411 amino acids
Theoretical weight: 47.51 KDa
Source organism: Leishmania major
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q4Q5S8 (Residues: 11-421; Coverage: 98%)
Gene names: LMJF_32_0080, NMT
Sequence domains:
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand MYA 1 x MYA

Cofactor: Ligand COA 1 x COA
4 bound ligands:
Ligand MG 1 x MG
Ligand EN5 1 x EN5
Ligand ENF 1 x ENF
Ligand DMS 2 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P21
Unit cell:
a: 48.659Å b: 91.131Å c: 53.777Å
α: 90° β: 113.85° γ: 90°
R-values:
R R work R free
0.174 0.173 0.205
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Drug target identification in protozoan parasites.
Müller et al. (2016)
2 more

3 mentions without citation

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