Research workbench
AlphaFold monomer V2.0 prediction for histone acetyltransferase type B subunit 2 (P0CS36)
Analyse AlphaFold monomer V2.0 prediction for histone acetyltransferase type B subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0CS36
- Type
- protein
- Length
- 435 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB44F19a0cb161828322eEEd13F55d4C3C34938d2
- Molecule
- Histone acetyltransferase type B subunit 2
- UniProt
- P0CS36
- Pockets
- 4 · best druggability 0.76
Structure
1 distinct chain · 14% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase type B subunit 2 | protein | 435 | 14% helix, 40% strand | P0CS36 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 415 | 0.76 | 0.85 | 34 | empty |
| 2 | 441 | 0.64 | 0.77 | 46 | empty |
| 3 | 148 | 0.49 | 0.78 | 14 | empty |
| 4 | 56 | 0.33 | 0.76 | 16 | empty |
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 P0CS36
- Elsewhere: UniProt P0CS36 · AlphaFold DB P0CS36
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