Research workbench
Crystal structure of asfv P15
Analyse Crystal structure of asfv P15 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BQ9
- Type
- protein
- Length
- 306 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 60 kda polyprotein
- UniProt
- A0A0A1DY09
- Pockets
- 4 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A | 60 kda polyprotein | protein | 153 | 28% helix, 23% strand | A0A0A1DY09 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 194 | 0.58 | 0.81 | 29 | empty |
| 2 | 65 | 0.55 | 0.88 | 23 | empty |
| 3 | 57 | 0.36 | 0.79 | 14 | empty |
| 4 | 81 | 0.34 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- B–A · 647 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 7BQ9 · Crystal structure of ASFV p15 · 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 A0A0A1DY09
- Elsewhere: RCSB PDB 7BQ9 · PDBe 7BQ9 · UniProt A0A0A1DY09
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