› 4cgm

X-ray diffraction
1.7Å resolution

Leishmania major N-myristoyltransferase in complex with a biphenyl- derivative inhibitor

Released:
DOI: 10.2210/pdb4cgm/pdb
PDB entry 4cgm coloured by chain, front view.
PDB entry 4cgm coloured by chain, side view.
PDB entry 4cgm coloured by chain, top view.
Source organism: Leishmania major
Primary publication:
Diverse modes of binding in structures of Leishmania major N-myristoyltransferase with selective inhibitors.
Brannigan JA, Roberts SM, Bell AS, Hutton JA, Hodgkinson MR, Tate EW, Leatherbarrow RJ, Smith DF, Wilkinson AJ
IUCrJ 1 250-60 (2014)
PMID: 25075346

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
2 bound ligands:
Ligand MG 1 x MG
Ligand CWZ 1 x CWZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21
Unit cell:
a: 48.46Å b: 92.093Å c: 53.636Å
α: 90° β: 113.71° γ: 90°
R-values:
R R work R free
0.188 0.185 0.246
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

New developments in probing and targeting protein acylation in malaria, leishmaniasis and African sleeping sickness.
Ritzefeld et al. (2018)
2 more

3 mentions without citation

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