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AlphaFold monomer V2.0 prediction for acetyltransferase (P16966)

Analyse AlphaFold monomer V2.0 prediction for acetyltransferase (P16966) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
P16966
Type
protein
Length
177 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x9188600a0FCa2914254C94299b1bd9721Bc4D500
Molecule
Acetyltransferase
UniProt
P16966
Pockets
1 · best druggability 0.65

Structure

1 distinct chain · 35% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAcetyltransferaseprotein17735% helix, 34% strandP16966

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13360.650.8032empty

Compared structures

  • 1GHE · Crystal structure of tabtoxin resistance protein complexed with an acyl coenzyme a · an experimental structure of the same protein · chain A against B, TM-score 0.96
  • 1GHE · Crystal structure of tabtoxin resistance protein complexed with an acyl coenzyme a · an experimental structure of the same protein · chain A against B, TM-score 0.96
  • 1J4J · Crystal Structure of Tabtoxin Resistance Protein (form II) complexed with an Acyl… · an experimental structure of the same protein · chain A against A, TM-score 0.95
  • 1J4J · Crystal structure of tabtoxin resistance protein (form II) complexed with an acyl… · an experimental structure of the same protein · chain A against A, TM-score 0.95

Analyse

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