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AlphaFold monomer V2.0 prediction for chaperone protein htpg (Q2JGG1)

Analyse AlphaFold monomer V2.0 prediction for chaperone protein htpg (Q2JGG1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
Q2JGG1
Type
protein
Length
650 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x362a6d063b1B7E1B6EfD3A9A7CA3612e3FE037AA
Molecule
Chaperone protein htpg
UniProt
Q2JGG1
Pockets
13 · best druggability 0.78

Structure

1 distinct chain · 38% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AChaperone protein htpgprotein65038% helix, 18% strandQ2JGG1

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13220.780.8946empty
2810.710.9525empty
3630.540.8818empty
42050.490.7626empty
51710.470.7632empty

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