Research workbench
Atomic model for bluetongue virus (btv) core
Analyse Atomic model for bluetongue virus (btv) core in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BTV
- Type
- protein
- Length
- 6,267 residues
- Chains
- 15
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (VP3 core protein); Protein (VP7 core protein)
- UniProt
- P56582, P18259
- Pockets
- 20 · best druggability 0.89
Structure
x-ray diffraction · 3 distinct chains · 40% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (VP3 core protein) | protein | 845 | 42% helix, 15% strand | P56582 |
| B | Protein (VP3 core protein) | protein | 885 | 40% helix, 13% strand | P56582 |
| P, C, D, Q, E, F, R, G, H, S, I, J, T | Protein (VP7 core protein) | protein | 349 | 34% helix, 19% strand | P18259 |
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 | 1037 | 0.89 | 0.91 | 144 | empty |
| 2 | 768 | 0.86 | 0.90 | 96 | empty |
| 3 | 754 | 0.86 | 0.89 | 49 | empty |
| 4 | 803 | 0.85 | 0.88 | 56 | empty |
| 5 | 791 | 0.85 | 0.88 | 41 | empty |
Interfaces
39 interfaces between chains.
- A–B · 2894 Ų buried · 34 hydrogen bonds · protein-protein
- P–D · 2727 Ų buried · 34 hydrogen bonds · protein-protein
- R–G · 2727 Ų buried · 39 hydrogen bonds · protein-protein
- S–I · 2720 Ų buried · 37 hydrogen bonds · protein-protein
- P–C · 2708 Ų buried · 36 hydrogen bonds · protein-protein
Compared structures
- 2BTV · Atomic model for bluetongue virus (btv) core · 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 P56582
- Every structure of UniProt P18259
- Elsewhere: RCSB PDB 2BTV · PDBe 2BTV · UniProt P56582 · UniProt P18259
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