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AlphaFold monomer V2.0 prediction for secreted rxlr effector protein 25 (A0A172M470)

Analyse AlphaFold monomer V2.0 prediction for secreted rxlr effector protein 25… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
A0A172M470
Type
protein
Length
416 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x7c75F0f7d6d136A2b8D4C6C6e9b3D8a697949DF1
Molecule
Secreted rxlr effector protein 25
Pockets
5 · best druggability 0.64

Structure

1 distinct chain · 66% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASecreted rxlr effector protein 25protein41666% helix, 0% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13690.640.7831empty
22910.510.7321empty
31170.370.7314empty
4810.360.7614empty
51030.330.7217empty

Analyse

  • Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure

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