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AlphaFold monomer V2.0 prediction for histone H2A-bbd type 2/3 (P0C5Z0)

Analyse AlphaFold monomer V2.0 prediction for histone H2A-bbd type 2/3 (P0C5Z0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
P0C5Z0
Type
protein
Length
115 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0xbb2F1C7CB3A1eeFAc24fCa72cc627162D5413FD7
UniProt
P0C5Z0

Structure

1 distinct chain.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein115—P0C5Z0

Compared structures

  • 6M4H · Structural mechanism of nucleosome dynamics governed by human histone variants H2A.B and… · an experimental structure of the same protein · chain A against G, TM-score 0.74
  • 6M4H · Structural mechanism of nucleosome dynamics governed by human histone variants H2A.B and… · an experimental structure of the same protein · chain A against C, TM-score 0.74
  • 6M4G · Structural mechanism of nucleosome dynamics governed by human histone variants H2A.B and… · an experimental structure of the same protein · chain A against G, TM-score 0.73
  • 6M4G · Structural mechanism of nucleosome dynamics governed by human histone variants H2A.B and… · an experimental structure of the same protein · chain A against C, TM-score 0.73
  • 6A7U · Crystal structure of histone H2A.Bbd-H2B dimer · an experimental structure of the same protein · chain A against A, TM-score 0.69
  • 6A7U · Crystal structure of histone H2A.BBD-H2B dimer · an experimental structure of the same protein · chain A against A, TM-score 0.69

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