Research workbench
Structure of the VPS75-RTT109 histone chaperone-lysine acetyltransferase complex (full-length proteins in space group P212121)
Analyse Structure of the VPS75-RTT109 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
- 3Q68
- Type
- protein
- Length
- 858 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vacuolar protein sorting-associated protein 75 (VPS75); Histone acetyltransferase RTT109
- EC
- 2.3.1.48
- UniProt
- P53853, Q07794
- Pockets
- 10 · best druggability 0.74
Structure
x-ray diffraction · 3 distinct chains · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar protein sorting-associated protein 75 (VPS75) | protein | 232 | 47% helix, 13% strand | P53853 |
| C | Histone acetyltransferase RTT109 (EC 2.3.1.48) | protein | 405 | 33% helix, 23% strand | Q07794 |
| B | Vacuolar protein sorting-associated protein 75 (VPS75) | protein | 221 | 51% helix, 14% strand | P53853 |
Pockets
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 708 | 0.74 | 0.80 | 89 | empty |
| 2 | 321 | 0.69 | 0.82 | 41 | empty |
| 3 | 241 | 0.65 | 0.83 | 31 | empty |
| 4 | 292 | 0.61 | 0.79 | 31 | empty |
| 5 | 255 | 0.54 | 0.77 | 48 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1865 Ų buried · 29 hydrogen bonds · protein-protein
- A–B · 1781 Ų buried · 7 hydrogen bonds · protein-protein
- C–B · 740 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (acetylation).
Compared structures
- 3Q68 · Structure of the Vps75-Rtt109 histone chaperone-lysine acetyltransferase complex… · the same entry in another collection · chain A against A, TM-score 1.00
- P53853 · AlphaFold monomer V2.0 prediction for vacuolar protein sorting- associated protein 75… · a predicted model of the same protein · chain B against A, TM-score 0.97
- Q07794 · AlphaFold monomer V2.0 prediction for histone acetyltransferase RTT109 (Q07794) · a predicted model of the same protein · chain C against A, TM-score 0.95
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
- Elsewhere: RCSB PDB 3Q68 · PDBe 3Q68 · UniProt P53853 · UniProt Q07794
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