Research workbench
C-terminal domain of capsid protein from bovine leukemia virus
Analyse C-terminal domain of capsid protein from bovine leukemia virus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PH1
- Type
- protein
- Length
- 228 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Blv capsid
- UniProt
- A7KWZ1
- Pockets
- 1 · best druggability 0.59
Structure
x-ray diffraction · 3 distinct chains · 61% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Blv capsid | protein | 73 | 63% helix, 0% strand | A7KWZ1 |
| B | Blv capsid | protein | 76 | 62% helix, 0% strand | A7KWZ1 |
| C | Blv capsid | protein | 79 | 58% helix, 0% strand | A7KWZ1 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 352 | 0.59 | 0.76 | 57 | empty |
Interfaces
3 interfaces between chains.
- A–B · 532 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 368 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 120 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4PH1 · C-terminal domain of capsid protein from bovine leukemia virus · 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 A7KWZ1
- Elsewhere: RCSB PDB 4PH1 · PDBe 4PH1 · UniProt A7KWZ1
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