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AlphaFold monomer V2.0 prediction for 10 kda chaperonin (B0VDR5)

Analyse AlphaFold monomer V2.0 prediction for 10 kda chaperonin (B0VDR5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
B0VDR5
Type
protein
Length
96 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x4b19F45398b689D52b4aF7DC26b26B77cd98f820
Molecule
10 kda chaperonin
UniProt
B0VDR5

Structure

1 distinct chain · 3% helix, 44% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A10 kda chaperoninprotein963% helix, 44% strandB0VDR5

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