Research workbench
Fitting of the bacteriophage PHI8 P1 capsid protein into cryo-EM density
Analyse Fitting of the bacteriophage PHI8 P1 capsid protein into cryo-EM density in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BX4
- Type
- protein
- Length
- 1,476 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- P1
- UniProt
- Q9MC13
- Pockets
- 20 · best druggability 0.80
Structure
electron microscopy · 1 distinct chain · 41% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | P1 | protein | 738 | 41% helix, 15% strand | Q9MC13 |
Pockets
20 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 839 | 0.80 | 0.83 | 87 | empty |
| 2 | 833 | 0.70 | 0.76 | 85 | empty |
| 3 | 143 | 0.69 | 0.88 | 20 | empty |
| 4 | 198 | 0.61 | 0.81 | 33 | empty |
| 5 | 207 | 0.58 | 0.80 | 31 | empty |
Interfaces
1 interface between chains.
- A–B · 1137 Ų buried · 46 hydrogen bonds · protein-protein
Compared structures
- 4BX4 · Fitting of the bacteriophage Phi8 P1 capsid protein into cryo-EM density · the same entry in another collection · chain B against B, 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 Q9MC13
- Elsewhere: RCSB PDB 4BX4 · PDBe 4BX4 · UniProt Q9MC13
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