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Crystal structure of human NAA50 in complex with accoa and an inhibitor (compound 4A) identified using DNA encoded library technology

Analyse Crystal structure of human NAA50 in complex with accoa and an inhibitor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6WFN
Type
protein
Length
151 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
N-alpha-acetyltransferase 50
EC
2.3.1.258, 2.3.1.-
UniProt
Q9GZZ1
Ligands
ACO, U2J
Pockets
1 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AN-alpha-acetyltransferase 50 (EC 2.3.1.258, 2.3.1.-)protein15132% helix, 36% strandQ9GZZ1

Ligands and binding sites

  • ACO · Acetyl coenzyme *A · ligand · chains A
  • U2J · (4S)-1-methyl-N-{(3S,5S)-5-[4-(methylcarbamoyl)-1,3-thiazol-2-yl]-1-[4-(1H-tetrazol-5-yl)benzene-1-carbonyl]pyrrolidin-3-yl}-2,6-dioxohexahydropyrimidine-4-carboxamide · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13330.630.7936ACO, U2J

Compared structures

  • 6WFN · Crystal structure of human Naa50 in complex with AcCoA and an inhibitor (compound 4a)… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9GZZ1 · AlphaFold monomer V2.0 prediction for N-alpha-acetyltransferase 50 (Q9GZZ1) · a predicted model of the same protein · chain A against A, TM-score 0.99

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