› 1iyl

X-ray diffraction
3.2Å resolution

Crystal Structure of Candida albicans N-myristoyltransferase with Non-peptidic Inhibitor

Released:
DOI: 10.2210/pdb1iyl/pdb
PDB entry 1iyl coloured by chain, front view.
PDB entry 1iyl coloured by chain, side view.
PDB entry 1iyl coloured by chain, top view.
Source organism: Candida albicans
Primary publication:
Crystal structures of Candida albicans N-myristoyltransferase with two distinct inhibitors.
Sogabe S, Masubuchi M, Sakata K, Fukami TA, Morikami K, Shiratori Y, Ebiike H, Kawasaki K, Aoki Y, Shimma N, D'Arcy A, Winkler FK, Banner DW, Ohtsuka T
Chem Biol 9 1119-28 (2002)
PMID: 12401496

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

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-151722 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycylpeptide N-tetradecanoyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
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 R64 3 x R64
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6B
Spacegroup: P212121
Unit cell:
a: 93.277Å b: 96.885Å c: 269.277Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.288 0.284 0.366
Expression system: Escherichia coli

Quick links

Citations

4 review citations

The protein as a variable in protein crystallization.
Dale et al. (2003)
3 more

32 mentions without citation

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