Research workbench
Crystal structure of rubella virus capsid protein (residues 127-277)
Analyse Crystal structure of rubella virus capsid protein (residues 127-277) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HBO
- Type
- protein
- Length
- 399 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Capsid protein
- UniProt
- Q8QL55
- Pockets
- 4 · best druggability 0.30
Structure
x-ray diffraction · 5 distinct chains · 7% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Capsid protein | protein | 79 | 9% helix, 39% strand | Q8QL55 |
| B | Capsid protein | protein | 76 | 0% helix, 42% strand | Q8QL55 |
| C | Capsid protein | protein | 82 | 10% helix, 37% strand | Q8QL55 |
| D | Capsid protein | protein | 81 | 6% helix, 41% strand | Q8QL55 |
| E | Capsid protein | protein | 81 | 9% helix, 47% strand | Q8QL55 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 61 | 0.30 | 0.74 | 10 | empty |
| 2 | 61 | 0.28 | 0.73 | 14 | empty |
| 3 | 54 | 0.26 | 0.73 | 13 | empty |
| 4 | 52 | 0.25 | 0.73 | 14 | empty |
Interfaces
5 interfaces between chains.
- B–E · 203 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 164 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 145 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 126 Ų buried · 1 hydrogen bond · protein-protein
- A–E · 15 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 4HBO · Crystal Structure of Rubella virus capsid protein (residues 127-277) · 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 Q8QL55
- Elsewhere: RCSB PDB 4HBO · PDBe 4HBO · UniProt Q8QL55
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