Human N-myristoyltransferase (NMT1) with myristoyl-CoA and imp-1088 inhibitor bound

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 29% strand (DSSP).

Ligands and binding sites

• MYA · Tetradecanoyl-coa · ligand · 2 copies · chains A, B
• KFK · 1-[5-[3,4-bis(fluoranyl)-2-[2-(1,3,5-trimethylpyrazol-4-yl)ethoxy]phenyl]-1-methyl-indazol-3-yl]-~{N},~{N}-dimethyl-methanamine · ligand · 2 copies · chains A, B
• MG · Magnesium ion · metal · 2 copies · chains A, B
• GOL · Glycerol · additive · 4 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 885 Ų buried · 22 hydrogen bonds · protein-protein

Compared structures

• 5MU6 · Human N-myristoyltransferase (NMT1) with Myristoyl-CoA and IMP-1088 inhibitor bound · the same entry in another collection · chain A against A, TM-score 1.00
• P30419 · AlphaFold monomer V2.0 prediction for glycylpeptide N-tetradecanoyltransferase 1 (P30419) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P30419
• Elsewhere: RCSB PDB 5MU6 · PDBe 5MU6 · UniProt P30419