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Structure of the mature rsv ca lattice: group IV, hexamer-hexamer interface, class 5'GAMMA
Analyse Structure of the mature rsv ca lattice: group IV, hexamer-hexamer interface… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NOQ
- Type
- protein
- Length
- 1,302 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Capsid protein P27, alternate cleaved 1
- UniProt
- P03322
- Pockets
- 13 · best druggability 0.52
Structure
electron microscopy · 3 distinct chains · 66% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, G, I | Capsid protein P27, alternate cleaved 1 | protein | 78 | 63% helix, 0% strand | P03322 |
| B, E | Capsid protein P27, alternate cleaved 1 | protein | 217 | 66% helix, 0% strand | P03322 |
| C, F, H, J | Capsid protein P27, alternate cleaved 1 | protein | 139 | 68% helix, 0% strand | P03322 |
Pockets
13 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 387 | 0.52 | 0.73 | 80 | empty |
| 2 | 378 | 0.51 | 0.72 | 70 | empty |
| 3 | 374 | 0.50 | 0.72 | 73 | empty |
| 4 | 361 | 0.50 | 0.72 | 71 | empty |
| 5 | 305 | 0.48 | 0.73 | 51 | empty |
Interfaces
11 interfaces between chains.
- B–C · 175 Ų buried · 0 hydrogen bonds · protein-protein
- E–F · 145 Ų buried · 0 hydrogen bonds · protein-protein
- A–E · 90 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 87 Ų buried · 0 hydrogen bonds · protein-protein
- D–G · 79 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7NOQ · Structure of the mature RSV CA lattice: Group IV, hexamer-hexamer interface, class 5'Gamma · 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 P03322
- Elsewhere: RCSB PDB 7NOQ · PDBe 7NOQ · UniProt P03322
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