Research workbench
Crystal structure of P domain of 485 norovirus
Analyse Crystal structure of P domain of 485 norovirus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4RPD
- Type
- protein
- Length
- 605 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Capsid protein
- UniProt
- Q20K66
- Pockets
- 4 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Capsid protein | protein | 302 | 6% helix, 36% strand | Q20K66 |
| B | Capsid protein | protein | 303 | 6% helix, 36% strand | Q20K66 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1115 | 0.80 | 0.81 | 128 | empty |
| 2 | 160 | 0.65 | 0.86 | 27 | empty |
| 3 | 63 | 0.33 | 0.76 | 15 | empty |
| 4 | 73 | 0.31 | 0.73 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1800 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 4RPD · Crystal Structure of P Domain of 485 Norovirus · 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 Q20K66
- Elsewhere: RCSB PDB 4RPD · PDBe 4RPD · UniProt Q20K66
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