Research workbench
The selenomethionine derivative of P3, the major coat protein of the lipid-containing bacteriophage PRD1.
Analyse The selenomethionine derivative of P3, the major coat protein of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HQN
- Type
- protein
- Length
- 1,111 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major capsid protein
- UniProt
- P22535
- Pockets
- 7 · best druggability 0.78
Structure
x-ray diffraction · 3 distinct chains · 14% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Major capsid protein | protein | 369 | 14% helix, 43% strand | P22535 |
| B | Major capsid protein | protein | 370 | 14% helix, 44% strand | P22535 |
| C | Major capsid protein | protein | 372 | 15% helix, 42% strand | P22535 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 577 | 0.78 | 0.84 | 45 | empty |
| 2 | 463 | 0.75 | 0.84 | 41 | empty |
| 3 | 562 | 0.75 | 0.82 | 48 | empty |
| 4 | 201 | 0.45 | 0.74 | 35 | empty |
| 5 | 120 | 0.45 | 0.78 | 22 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1770 Ų buried · 32 hydrogen bonds · protein-protein
- A–C · 1758 Ų buried · 36 hydrogen bonds · protein-protein
- A–B · 1737 Ų buried · 37 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 15 modified (engineered).
Compared structures
- 1HQN · The selenomethionine derivative of P3, the major coat protein of the lipid-containing… · 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 P22535
- Elsewhere: RCSB PDB 1HQN · PDBe 1HQN · UniProt P22535
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