MolNFT v1 · #19156 · protein
Bacteriophage Q beta capsid
1QBE: “Bacteriophage Q beta capsid”. X-ray diffraction, 2 pockets (best druggability 0.74). MolNFT v1 #19156 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1QBE
- Type
- protein
- Length
- 378 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bacteriophage Q beta capsid
- UniProt
- P03615
- Pockets
- 2 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Bacteriophage Q beta capsid | protein | 123 | 21% helix, 46% strand | P03615 |
| B | Bacteriophage Q beta capsid | protein | 132 | 20% helix, 42% strand | P03615 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1043 | 0.74 | 0.77 | 117 | empty |
| 2 | 56 | 0.27 | 0.72 | 12 | empty |
Interfaces
3 interfaces between chains.
- B–C · 499 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 462 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 451 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 1QBE · Bacteriophage Q beta capsid · the same entry in another collection · chain C against C, 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 P03615
- Elsewhere: RCSB PDB 1QBE · PDBe 1QBE · UniProt P03615
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