Research workbench
Structure of Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate.
Analyse Structure of Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6O22
- Type
- protein
- Length
- 1,192 residues
- Chains
- 6
- Method
- solution nmr, solution scattering
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- NOT
- Source
- Saccharomyces cerevisiae (strain ATCC 204508 / S288c); Xenopus laevis
- Molecule
- Vacuolar protein sorting-associated protein 75; Histone acetyltransferase RTT109; Histone…
- EC
- 2.3.1.48
- UniProt
- P53853, Q07794, P32447, P84233, P62799
- Pockets
- 15 · best druggability 0.79
Structure
solution nmr, solution scattering · resolution NOT · 6 distinct chains · 37% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar protein sorting-associated protein 75 | protein | 230 | 45% helix, 13% strand | P53853 |
| B | Vacuolar protein sorting-associated protein 75 | protein | 217 | 42% helix, 14% strand | P53853 |
| C | Histone acetyltransferase RTT109 (EC 2.3.1.48) | protein | 424 | 33% helix, 21% strand | Q07794 |
| D | Histone chaperone ASF1 | protein | 164 | 7% helix, 46% strand | P32447 |
| E | Histone H3.2 | protein | 75 | 68% helix, 5% strand | P84233 |
| F | Histone H4 | protein | 82 | 57% helix, 9% strand | P62799 |
Pockets
15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1148 | 0.79 | 0.80 | 93 | empty |
| 2 | 574 | 0.75 | 0.82 | 73 | empty |
| 3 | 773 | 0.72 | 0.78 | 78 | empty |
| 4 | 169 | 0.62 | 0.84 | 38 | empty |
| 5 | 225 | 0.57 | 0.79 | 29 | empty |
Interfaces
10 interfaces between chains.
- E–F · 2320 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 1750 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 1643 Ų buried · 43 hydrogen bonds · protein-protein
- D–E · 1092 Ų buried · 18 hydrogen bonds · protein-protein
- B–C · 923 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 6O22 · Structure of ASF1-H3:H4-RTT109-VPS75 histone chaperone-lysine acetyltransferase complex… · the same entry in another collection · chain F against F, TM-score 1.00
- P32447 · AlphaFold monomer V2.0 prediction for histone chaperone ASF1 (P32447) · a predicted model of the same protein · chain D against A, TM-score 0.97
- P84233 · AlphaFold monomer V2.0 prediction for histone H3.2 (P84233) · a predicted model of the same protein · chain E against A, TM-score 0.93
- Q07794 · AlphaFold monomer V2.0 prediction for histone acetyltransferase RTT109 (Q07794) · a predicted model of the same protein · chain C against A, TM-score 0.89
- P53853 · AlphaFold monomer V2.0 prediction for vacuolar protein sorting- associated protein 75… · a predicted model of the same protein · chain A against A, TM-score 0.89
- P62799 · AlphaFold monomer V2.0 prediction for histone H4 (P62799) · a predicted model of the same protein · chain F against A, TM-score 0.81
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 P53853
- Every structure of UniProt Q07794
- Every structure of UniProt P32447
- Every structure of UniProt P84233
- Every structure of UniProt P62799
- Elsewhere: RCSB PDB 6O22 · PDBe 6O22 · UniProt P53853 · UniProt Q07794 · UniProt P32447 · UniProt P84233 · UniProt P62799
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