Research workbench
The protein of cat virus
Analyse The protein of cat virus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LP9
- Type
- protein
- Length
- 416 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NSP1 protein
- UniProt
- V9PIT5
- Pockets
- 3 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 19% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A, C, D | NSP1 protein | protein | 104 | 19% helix, 45% strand | V9PIT5 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 308 | 0.55 | 0.75 | 37 | empty |
| 2 | 120 | 0.52 | 0.81 | 19 | empty |
| 3 | 108 | 0.49 | 0.81 | 24 | empty |
Interfaces
4 interfaces between chains.
- B–A · 753 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 744 Ų buried · 12 hydrogen bonds · protein-protein
- A–D · 341 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 332 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 6LP9 · the protein of cat virus · 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 V9PIT5
- Elsewhere: RCSB PDB 6LP9 · PDBe 6LP9 · UniProt V9PIT5
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