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AlphaFold monomer V2.0 prediction for chaperone protein htpg (B8F5X3)

Analyse AlphaFold monomer V2.0 prediction for chaperone protein htpg (B8F5X3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
B8F5X3
Type
protein
Length
628 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x3A9BC68142273081F4d4e5b4B741fB34F3E13225
Molecule
Chaperone protein htpg
UniProt
B8F5X3
Pockets
8 · best druggability 0.75

Structure

1 distinct chain · 44% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AChaperone protein htpgprotein62844% helix, 22% strandB8F5X3

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18160.750.7973empty
2580.520.8719empty
31820.520.7824empty
41100.400.7516empty
5610.380.7914empty

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