Research workbench
Structure of viral protein BKRF4 in complex with H2A-H2B
Analyse Structure of viral protein BKRF4 in complex with H2A-H2B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7VCL
- Type
- protein
- Length
- 185 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone H2A-H2B; Tegument protein BKRF4
- UniProt
- Q3KSS1
- Pockets
- 1 · best druggability 0.39
Structure
x-ray diffraction · 2 distinct chains · 69% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone H2A-H2B | protein | 177 | 72% helix, 3% strand | — |
| B | Tegument protein BKRF4 | protein | 8 | 0% helix, 13% strand | Q3KSS1 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 108 | 0.39 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 374 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 7VCL · structure of viral protein BKRF4 in complex with H2A-H2B · 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 Q3KSS1
- Elsewhere: RCSB PDB 7VCL · PDBe 7VCL · UniProt Q3KSS1
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