Research workbench
Three-dimensional structure of theiler virus
Analyse Three-dimensional structure of theiler virus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TME
- Type
- protein
- Length
- 766 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- THEILER'S murine encephalomyelitis virus (subunit VP1); THEILER'S murine…
- UniProt
- P13899
- Pockets
- 11 · best druggability 0.66
Structure
x-ray diffraction · 4 distinct chains · 8% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 1 | THEILER'S murine encephalomyelitis virus (subunit VP1) | protein | 256 | 6% helix, 32% strand | P13899 |
| 2 | THEILER'S murine encephalomyelitis virus (subunit VP2) | protein | 255 | 11% helix, 39% strand | P13899 |
| 3 | THEILER'S murine encephalomyelitis virus (subunit VP3) | protein | 230 | 7% helix, 36% strand | P13899 |
| 4 | THEILER'S murine encephalomyelitis virus (subunit VP4) | protein | 25 | 16% helix, 8% strand | P13899 |
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 51 | 0.66 | 0.96 | 16 | empty |
| 2 | 320 | 0.63 | 0.79 | 40 | empty |
| 3 | 254 | 0.58 | 0.78 | 28 | empty |
| 4 | 216 | 0.52 | 0.77 | 33 | empty |
| 5 | 162 | 0.49 | 0.77 | 22 | empty |
Interfaces
6 interfaces between chains.
- 1–3 · 3453 Ų buried · 45 hydrogen bonds · protein-protein
- 1–2 · 2277 Ų buried · 32 hydrogen bonds · protein-protein
- 2–3 · 1648 Ų buried · 18 hydrogen bonds · protein-protein
- 3–4 · 722 Ų buried · 12 hydrogen bonds · protein-protein
- 1–4 · 431 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 1TME · Three-dimensional structure of theiler virus · the same entry in another collection · chain 1 against 1, 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 P13899
- Elsewhere: RCSB PDB 1TME · PDBe 1TME · UniProt P13899
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