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AlphaFold monomer V2.0 prediction for thymidylate synthase (A6VMA0)

Analyse AlphaFold monomer V2.0 prediction for thymidylate synthase (A6VMA0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
A6VMA0
Type
protein
Length
283 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0xd1A2963012bEcbC7A8f505464439Ab678C48936f
Molecule
Thymidylate synthase
UniProt
A6VMA0
Pockets
2 · best druggability 0.72

Structure

1 distinct chain · 38% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AThymidylate synthaseprotein28338% helix, 25% strandA6VMA0

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14470.720.8247empty
2550.290.7512empty

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