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AlphaFold monomer V2.0 prediction for phosphate acetyltransferase (P38503)

Analyse AlphaFold monomer V2.0 prediction for phosphate acetyltransferase (P38503) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
P38503
Type
protein
Length
333 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0xA7381fE9bA15c95992d24BC2A3Bb44aB0Cd83e3f
Molecule
Phosphate acetyltransferase
UniProt
P38503
Pockets
3 · best druggability 0.50

Structure

1 distinct chain · 46% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhosphate acetyltransferaseprotein33346% helix, 16% strandP38503

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11690.500.7721empty
21090.390.7423empty
3810.350.7620empty

Compared structures

  • 1QZT · Phosphotransacetylase from Methanosarcina thermophila · an experimental structure of the same protein · chain A against B, TM-score 0.99
  • 1QZT · Phosphotransacetylase from methanosarcina thermophila · an experimental structure of the same protein · chain A against B, TM-score 0.99
  • 2AF4 · Phosphotransacetylase from methanosarcina thermophila co- crystallized with coenzyme a · an experimental structure of the same protein · chain A against D, TM-score 0.93
  • 2AF4 · Phosphotransacetylase from Methanosarcina thermophila co-crystallized with coenzyme A · an experimental structure of the same protein · chain A against D, TM-score 0.93
  • 2AF3 · Phosphotransacetylase from Methanosarcina thermophila soaked with Coenzyme A · an experimental structure of the same protein · chain A against C, TM-score 0.91
  • 2AF3 · Phosphotransacetylase from methanosarcina thermophila soaked with coenzyme a · an experimental structure of the same protein · chain A against C, TM-score 0.91

Analyse

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