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X-ray diffraction
1.8Å resolution

CRYSTAL STRUCTURE OF LEISHMANIA MAJOR N-MYRISTOYLTRANSFERASE (NMT) WITH BOUND MYRISTOYL-COA AND A FRAGMENT

Released:
DOI: 10.2210/pdb4ucn/pdb
PDB entry 4ucn coloured by chain, front view.
PDB entry 4ucn coloured by chain, side view.
PDB entry 4ucn coloured by chain, top view.
Source organism: Leishmania major
Primary publication:
Identification and structure solution of fragment hits against kinetoplastid N-myristoyltransferase.
Robinson DA, Wyatt PG
Acta Crystallogr F Struct Biol Commun 71 586-93 (2015)
PMID: 25945713

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: 438 amino acids
Theoretical weight: 50.51 KDa
Source organism: Leishmania major
Expression system: Escherichia coli
UniProt:
  • Canonical: Q4Q5S8 (Residues: 5-421; Coverage: 99%)
Gene names: LMJF_32_0080, NMT
Sequence domains:
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand MYA 1 x MYA
1 bound ligand:
Ligand JRB 1 x JRB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P21
Unit cell:
a: 47.28Å b: 91.23Å c: 52.96Å
α: 90° β: 112.33° γ: 90°
R-values:
R R work R free
0.17 0.168 0.2
Expression system: Escherichia coli

Quick links

Citations

1 mention without citation

Identification and structure solution of fragment hits against kinetoplastid N-myristoyltransferase.
Robinson et al. (2015)