MolNFT v1 · #50914 · protein
Structure of tomato bushy stunt virus. V. coat protein sequence determination and its structural implications
2TBV: “Structure of tomato bushy stunt virus. V. coat protein sequence determination and its structural implications”. X-ray diffraction, 1 ligand (CA), 9 pockets (best druggability 0.72). MolNFT v1 #50914 on GenesisL1: 3D structure…
- PDB
- 2TBV
- Type
- protein
- Length
- 893 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tomato bushy stunt virus
- UniProt
- P11795
- Ligands
- CA
- Pockets
- 9 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 2% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Tomato bushy stunt virus | protein | 286 | 2% helix, 40% strand | P11795 |
| C | Tomato bushy stunt virus | protein | 321 | 2% helix, 36% strand | P11795 |
Ligands and binding sites
- CA · Calcium ion · metal · 6 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 410 | 0.72 | 0.82 | 39 | empty |
| 2 | 212 | 0.67 | 0.85 | 40 | empty |
| 3 | 235 | 0.66 | 0.84 | 38 | empty |
| 4 | 330 | 0.59 | 0.77 | 45 | CA |
| 5 | 225 | 0.59 | 0.80 | 31 | empty |
Interfaces
3 interfaces between chains.
- A–B · 717 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 709 Ų buried · 20 hydrogen bonds · protein-protein
- B–C · 634 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 2TBV · Structure of tomato bushy stunt virus. V. coat protein sequence determination and its… · the same entry in another collection · chain B against B, 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 P11795
- Elsewhere: RCSB PDB 2TBV · PDBe 2TBV · UniProt P11795
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