Research workbench
Melbournevirus nucleosome like particle
Analyse Melbournevirus nucleosome like particle in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7N8N
- Type
- protein + DNA
- Length
- 1,048 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone H4-H3 doublet; Histone H2B-H2A doublet; DNA (147-mer)
- UniProt
- A0A097I2D0, A0A097I2B5
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 4 distinct chains · 59% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Histone H4-H3 doublet | protein | 197 | 55% helix, 3% strand | A0A097I2D0 |
| B, D | Histone H2B-H2A doublet | protein | 202 | 63% helix, 2% strand | A0A097I2B5 |
| I | DNA (147-mer) | dna | 125 | — | — |
| J | DNA (147-mer) | dna | 125 | — | — |
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 | 753 | 0.85 | 0.88 | 125 | empty |
| 2 | 844 | 0.79 | 0.83 | 71 | empty |
| 3 | 247 | 0.78 | 0.90 | 56 | empty |
| 4 | 793 | 0.77 | 0.81 | 60 | empty |
| 5 | 837 | 0.72 | 0.78 | 73 | empty |
Interfaces
15 interfaces between chains.
- I–J · 5634 Ų buried · 583 hydrogen bonds · nucleic-nucleic
- B–C · 1132 Ų buried · 24 hydrogen bonds · protein-protein
- A–D · 1123 Ų buried · 24 hydrogen bonds · protein-protein
- C–I · 867 Ų buried · 38 hydrogen bonds · protein-nucleic
- A–J · 814 Ų buried · 31 hydrogen bonds · protein-nucleic
Compared structures
- 7N8N · Melbournevirus nucleosome like particle · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A097I2D0
- Every structure of UniProt A0A097I2B5
- Elsewhere: RCSB PDB 7N8N · PDBe 7N8N · UniProt A0A097I2D0 · UniProt A0A097I2B5
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