Research workbench
P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: stability without auxiliary proteins or chemical cross-links
Analyse P22 procapsid coat protein structures reveal a novel mechanism for capsid… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3IYH
- Type
- protein
- Length
- 2,346 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Coat protein
- UniProt
- P26747
- Pockets
- 6 · best druggability 0.55
Structure
electron microscopy · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Coat protein | protein | 391 | 0% helix, 0% strand | P26747 |
Pockets
6 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 263 | 0.55 | 0.74 | 57 | empty |
| 2 | 254 | 0.54 | 0.74 | 52 | empty |
| 3 | 245 | 0.53 | 0.74 | 52 | empty |
| 4 | 255 | 0.53 | 0.74 | 60 | empty |
| 5 | 242 | 0.52 | 0.74 | 52 | empty |
Interfaces
6 interfaces between chains.
- E–F · 274 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 239 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 206 Ų buried · 0 hydrogen bonds · protein-protein
- D–E · 189 Ų buried · 0 hydrogen bonds · protein-protein
- C–D · 176 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3IYH · P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation… · 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 P26747
- Elsewhere: RCSB PDB 3IYH · PDBe 3IYH · UniProt P26747
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