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Solution structure of the BHRF1 protein from epstein-barr virus, a homolog of human BCL-2
Analyse Solution structure of the BHRF1 protein from epstein-barr virus, a homolog of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Q59
- Type
- protein
- Length
- 172 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Early antigen protein R
- UniProt
- P03182
- Pockets
- 5 · best druggability 0.74
Structure
solution nmr · 1 distinct chain · 53% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Early antigen protein R | protein | 172 | 53% helix, 0% strand | P03182 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 79 | 0.74 | 0.97 | 14 | empty |
| 2 | 123 | 0.41 | 0.75 | 26 | empty |
| 3 | 56 | 0.39 | 0.80 | 10 | empty |
| 4 | 69 | 0.33 | 0.75 | 17 | empty |
| 5 | 64 | 0.29 | 0.73 | 13 | empty |
Compared structures
- 1Q59 · Solution Structure of the BHRF1 Protein From Epstein-Barr Virus, a Homolog of Human Bcl-2 · 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 P03182
- Elsewhere: RCSB PDB 1Q59 · PDBe 1Q59 · UniProt P03182
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