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AlphaFold monomer V2.0 prediction for chaperone protein CLPB3, mitochondrial (Q0E3C8)

Analyse AlphaFold monomer V2.0 prediction for chaperone protein CLPB3, mitochondrial… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
Q0E3C8
Type
protein
Length
983 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x9823334B175F9f2683922fd5F25c4D9e96Fd15E9
Molecule
Chaperone protein CLPB3, mitochondrial
UniProt
Q0E3C8
Pockets
9 · best druggability 0.62

Structure

1 distinct chain · 54% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AChaperone protein CLPB3, mitochondrialprotein98354% helix, 10% strandQ0E3C8

Pockets

9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12860.620.8027empty
21450.600.8426empty
31780.520.7823empty
42150.510.7728empty
5540.390.8110empty

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