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AlphaFold monomer V2.0 prediction for 2-epi-5-epi-valiolone synthase (H2K887)

Analyse AlphaFold monomer V2.0 prediction for 2-epi-5-epi-valiolone synthase (H2K887) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
H2K887
Type
protein
Length
414 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0xa73BAb1DabE4333A884D03393eAa10c3B4215494
Molecule
2-epi-5-epi-valiolone synthase
UniProt
H2K887
Pockets
2 · best druggability 0.79

Structure

1 distinct chain · 48% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A2-epi-5-epi-valiolone synthaseprotein41448% helix, 18% strandH2K887

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16030.790.8569empty
2860.310.7317empty

Compared structures

  • 4P53 · ValA (2-epi-5-epi-valiolone synthase) from Streptomyces hygroscopicus subsp.… · an experimental structure of the same protein · chain A against A, TM-score 0.87
  • 4P53 · Vala (2-epi-5-epi-valiolone synthase) from streptomyces hygroscopicus subsp.… · an experimental structure of the same protein · chain A against A, TM-score 0.87

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