› 5g21

X-ray diffraction
1.5Å resolution

Leishmania major N-myristoyltransferase in complex with a quinoline inhibitor (compound 26).

Released:
DOI: 10.2210/pdb5g21/pdb
Model geometry
Fit model/data
PDB entry 5g21 coloured by chain, front view.
PDB entry 5g21 coloured by chain, side view.
PDB entry 5g21 coloured by chain, top view.
Source organism: Leishmania major
Primary publication:
Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase.
Goncalves V, Brannigan JA, Laporte A, Bell AS, Roberts SM, Wilkinson AJ, Leatherbarrow RJ, Tate EW
OpenAccess logo Medchemcomm 8 191-197 (2017)
PMID: 28626547

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 YN4 1 x YN4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P21
Unit cell:
a: 48.676Å b: 91.068Å c: 53.571Å
α: 90° β: 114.55° γ: 90°
R-values:
R R work R free
0.176 0.174 0.209
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Drug discovery in leishmaniasis using protein lipidation as a target.
Brannigan et al. (2021)
1 more

1 mention without citation

Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase.
Goncalves et al. (2017)