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

Structure

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

Ligands and binding sites

• BXN · 4-[3-[(8~{A}~{R})-3,4,6,7,8,8~{A}-hexahydro-1~{H}-pyrrolo[1,2-a]pyrazin-2-yl]propyl]-2,6-bis(chloranyl)-~{N}-methyl-~{N}-(1,3,5-trimethylpyrazol-4-yl) benzenesulfonamide · ligand · 2 copies · chains A, B
• MYA · Tetradecanoyl-coa · 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

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 932 Ų buried · 23 hydrogen bonds · protein-protein

Compared structures

• 6FZ5 · Human N-myristoyltransferase (NMT1) with Myristoyl-CoA and 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 6FZ5 · PDBe 6FZ5 · UniProt P30419