Research workbench
Class 3 : translocated nucleosome
Analyse Class 3 : translocated nucleosome in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FQ8
- Type
- protein + DNA
- Length
- 1,038 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone H3.3C; Histone H4; Histone H2A; Histone H2B; DNA (147-mer)
- UniProt
- P02302, P62799, Q6AZJ8, A0A1L8FQ56
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 9 distinct chains · 64% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone H3.3C | protein | 95 | 66% helix, 4% strand | P02302 |
| B | Histone H4 | protein | 84 | 64% helix, 7% strand | P62799 |
| C | Histone H2A | protein | 105 | 56% helix, 6% strand | Q6AZJ8 |
| D, H | Histone H2B | protein | 89 | 78% helix, 4% strand | A0A1L8FQ56 |
| E | Histone H3.3C | protein | 93 | 68% helix, 4% strand | P02302 |
| F | Histone H4 | protein | 83 | 63% helix, 7% strand | P62799 |
| G | Histone H2A | protein | 106 | 54% helix, 6% strand | Q6AZJ8 |
| I | DNA (147-mer) | dna | 147 | — | — |
| J | DNA (147-mer) | dna | 147 | — | — |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1096 | 0.85 | 0.86 | 142 | empty |
| 2 | 356 | 0.78 | 0.88 | 53 | empty |
| 3 | 573 | 0.71 | 0.80 | 59 | empty |
| 4 | 901 | 0.68 | 0.74 | 69 | empty |
| 5 | 529 | 0.65 | 0.77 | 33 | empty |
Interfaces
37 interfaces between chains.
- I–J · 6820 Ų buried · 746 hydrogen bonds · nucleic-nucleic
- G–H · 2548 Ų buried · 20 hydrogen bonds · protein-protein
- C–D · 2466 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 2451 Ų buried · 17 hydrogen bonds · protein-protein
- E–F · 2412 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
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 P02302
- Every structure of UniProt P62799
- Every structure of UniProt Q6AZJ8
- Every structure of UniProt A0A1L8FQ56
- Elsewhere: RCSB PDB 6FQ8 · PDBe 6FQ8 · UniProt P02302 · UniProt P62799 · UniProt Q6AZJ8 · UniProt A0A1L8FQ56
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