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X-ray diffraction
1.42Å resolution

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-111913 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycylpeptide N-tetradecanoyltransferase Chain: A
Molecule details ›
Chain: A
Length: 421 amino acids
Theoretical weight: 48.66 KDa
Source organism: Leishmania donovani
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: D0AB09 (Residues: 1-421; Coverage: 100%)
Gene name: nmt
Sequence domains:
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand NHW 1 x NHW
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 45.97Å b: 90.131Å c: 92.355Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.149 0.146 0.191
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

Fatty acylation of proteins: The long and the short of it.
Resh MD. (2016)
9 more

13 mentions without citation

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