Research workbench
EBV tegument protein BBRF2
Analyse EBV tegument protein BBRF2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LQN
- Type
- protein
- Length
- 263 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.60002
- Source
- Human gammaherpesvirus 4
- Molecule
- Cytoplasmic envelopment protein 1
- UniProt
- K9US56
- Ligands
- SO4, NO3
Structure
x-ray diffraction · resolution 1.60002 · 1 distinct chain · 48% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytoplasmic envelopment protein 1 | protein | 263 | 48% helix, 17% strand | K9US56 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 9 modified (engineered).
Compared structures
- 6LQN · EBV tegument protein BBRF2 · 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
- Elsewhere: RCSB PDB 6LQN · PDBe 6LQN · UniProt K9US56
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