Research workbench
Cricket paralysis virus (crpv)
Analyse Cricket paralysis virus (crpv) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1B35
- Type
- protein
- Length
- 854 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (cricket paralysis virus, VP1); Protein (cricket paralysis virus, VP2); Protein…
- UniProt
- P13418
- Pockets
- 9 · best druggability 0.69
Structure
x-ray diffraction · 4 distinct chains · 16% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (cricket paralysis virus, VP1) | protein | 260 | 15% helix, 33% strand | P13418 |
| B | Protein (cricket paralysis virus, VP2) | protein | 255 | 16% helix, 38% strand | P13418 |
| C | Protein (cricket paralysis virus, VP3) | protein | 282 | 12% helix, 32% strand | P13418 |
| D | Protein (cricket paralysis virus, VP4) | protein | 57 | 33% helix, 0% strand | P13418 |
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 414 | 0.69 | 0.81 | 58 | empty |
| 2 | 183 | 0.61 | 0.83 | 27 | empty |
| 3 | 205 | 0.50 | 0.76 | 38 | empty |
| 4 | 76 | 0.49 | 0.83 | 19 | empty |
| 5 | 122 | 0.43 | 0.77 | 16 | empty |
Interfaces
4 interfaces between chains.
- A–C · 4211 Ų buried · 56 hydrogen bonds · protein-protein
- B–C · 1815 Ų buried · 25 hydrogen bonds · protein-protein
- A–B · 1159 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 238 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1B35 · Cricket paralysis virus (crpv) · 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 P13418
- Elsewhere: RCSB PDB 1B35 · PDBe 1B35 · UniProt P13418
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