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Human N-myristoyltransferase (NMT1) with myristoyl-CoA co-factor

Analyse Human N-myristoyltransferase (NMT1) with myristoyl-CoA co-factor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4C2Y
Type
protein
Length
764 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glycylpeptide N-tetradecanoyltransferase 1
EC
2.3.1.97
UniProt
P30419
Ligands
MYA, MG
Pockets
5 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BGlycylpeptide N-tetradecanoyltransferase 1 (EC 2.3.1.97)protein38227% helix, 28% strandP30419

Ligands and binding sites

  • MYA · Tetradecanoyl-coa · ligand · 2 copies · chains A, B
  • MG · Magnesium ion · metal · 2 copies · chains A, B
  • GOL · Glycerol · additive · 7 copies · chains A, B
  • CIT · Citric acid · additive · 2 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110480.790.8092MYA, MG, GOL
29970.790.8089MYA, MG, GOL
38430.770.8072GOL
4690.350.7715CIT
5520.320.7715CIT

Interfaces

1 interface between chains.

  • A–B · 901 Ų buried · 23 hydrogen bonds · protein-protein

Compared structures

  • 4C2Y · Human N-myristoyltransferase (NMT1) with Myristoyl-CoA co-factor · 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

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