Research workbench
AlphaFold monomer V2.0 prediction for core histone macro-H2A.1 (O75367)
Analyse AlphaFold monomer V2.0 prediction for core histone macro-H2A.1 (O75367) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O75367
- Type
- protein
- Length
- 372 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB44F19a0cb161828322eEEd13F55d4C3C34938d2
- Molecule
- Core histone macro-H2A.1
- UniProt
- O75367
- Pockets
- 3 · best druggability 0.56
Structure
1 distinct chain · 37% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Core histone macro-H2A.1 | protein | 372 | 37% helix, 10% strand | O75367 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 174 | 0.56 | 0.81 | 23 | empty |
| 2 | 93 | 0.39 | 0.76 | 22 | empty |
| 3 | 69 | 0.29 | 0.73 | 13 | empty |
Compared structures
- 5IIT · Structure of spx domain of the yeast inorganic polyphophate polymerase VTC4 crystallized… · an experimental structure of the same protein · chain A against C, TM-score 0.54
- 5IIT · Structure of SPX domain of the yeast inorganic polyphophate polymerase Vtc4 crystallized… · an experimental structure of the same protein · chain A against C, TM-score 0.54
- 5LNC · Structure of spx domain of the yeast inorganic polyphophate polymerase VTC4 crystallized… · an experimental structure of the same protein · chain A against B, TM-score 0.52
- 5LNC · Structure of SPX domain of the yeast inorganic polyphophate polymerase Vtc4 crystallized… · an experimental structure of the same protein · chain A against B, TM-score 0.52
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O75367
- Elsewhere: UniProt O75367 · AlphaFold DB O75367
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