› 1nmt

X-ray diffraction
2.45Å resolution

N-MYRISTOYL TRANSFERASE FROM CANDIDA ALBICANS AT 2.45 A

Released:
DOI: 10.2210/pdb1nmt/pdb
PDB entry 1nmt coloured by chain, front view.
PDB entry 1nmt coloured by chain, side view.
PDB entry 1nmt coloured by chain, top view.
Source organism: Candida albicans
Primary publication:
Crystal structure of the anti-fungal target N-myristoyl transferase.
Weston SA, Camble R, Colls J, Rosenbrock G, Taylor I, Egerton M, Tucker AD, Tunnicliffe A, Mistry A, Mancia F, de la Fortelle E, Irwin J, Bricogne G, Pauptit RA
Nat Struct Biol 5 213-21 (1998)
PMID: 9501915

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:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151724 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycylpeptide N-tetradecanoyltransferase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 392 amino acids
Theoretical weight: 45.42 KDa
Source organism: Candida albicans
Expression system: Escherichia coli
UniProt:
  • Canonical: P30418 (Residues: 60-451; Coverage: 87%)
Gene names: CAALFM_C401440WA, CaO19.12111, CaO19.4641, NMT1
Sequence domains:
Structure domains: Aminopeptidase

Ligands and Environments

1 bound ligand:
Ligand GOL 18 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: C2221
Unit cell:
a: 132Å b: 166.5Å c: 179.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.214 0.251
Expression system: Escherichia coli

Quick links

Citations

24 review citations

Histone acetyltransferases.
Roth et al. (2001)
23 more

7 mentions without citation

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