Research workbench
EBV tegument protein BBRF2/BSRF1 complex
Analyse EBV tegument protein BBRF2/BSRF1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LQO
- Type
- protein
- Length
- 2,053 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytoplasmic envelopment protein 1; Tegument protein UL51 homolog
- UniProt
- K9US56, P0CK62
- Pockets
- 20 · best druggability 0.74
Structure
x-ray diffraction · 12 distinct chains · 56% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytoplasmic envelopment protein 1 | protein | 258 | 49% helix, 16% strand | K9US56 |
| B | Cytoplasmic envelopment protein 1 | protein | 254 | 49% helix, 16% strand | K9US56 |
| C | Cytoplasmic envelopment protein 1 | protein | 242 | 49% helix, 17% strand | K9US56 |
| D | Cytoplasmic envelopment protein 1 | protein | 254 | 48% helix, 17% strand | K9US56 |
| E | Cytoplasmic envelopment protein 1 | protein | 257 | 49% helix, 16% strand | K9US56 |
| F | Cytoplasmic envelopment protein 1 | protein | 255 | 47% helix, 16% strand | K9US56 |
| H | Tegument protein UL51 homolog | protein | 91 | 76% helix, 0% strand | P0CK62 |
| I | Tegument protein UL51 homolog | protein | 88 | 74% helix, 0% strand | P0CK62 |
| J | Tegument protein UL51 homolog | protein | 93 | 76% helix, 0% strand | P0CK62 |
| K | Tegument protein UL51 homolog | protein | 81 | 80% helix, 0% strand | P0CK62 |
| L | Tegument protein UL51 homolog | protein | 94 | 81% helix, 0% strand | P0CK62 |
| M | Tegument protein UL51 homolog | protein | 86 | 80% helix, 0% strand | P0CK62 |
Ligands and binding sites
- ACT · Acetate ion · additive · 3 copies · chains C, J, E, K, A, H
- GOL · Glycerol · additive · 3 copies · chains C, I, J, E, K, F, M
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 450 | 0.74 | 0.83 | 42 | empty |
| 2 | 293 | 0.74 | 0.87 | 37 | ACT, GOL |
| 3 | 1169 | 0.74 | 0.77 | 103 | empty |
| 4 | 372 | 0.74 | 0.85 | 36 | empty |
| 5 | 369 | 0.71 | 0.83 | 46 | empty |
Interfaces
30 interfaces between chains.
- B–I · 1411 Ų buried · 10 hydrogen bonds · protein-protein
- C–J · 1397 Ų buried · 8 hydrogen bonds · protein-protein
- F–L · 1392 Ų buried · 9 hydrogen bonds · protein-protein
- A–H · 1376 Ų buried · 9 hydrogen bonds · protein-protein
- D–M · 1355 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 6LQO · EBV tegument protein BBRF2/BSRF1 complex · 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 K9US56
- Every structure of UniProt P0CK62
- Elsewhere: RCSB PDB 6LQO · PDBe 6LQO · UniProt K9US56 · UniProt P0CK62
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