Research workbench
Crystal structure of the truncated EBV BFRF1-BFLF2 nuclear egress complex
Analyse Crystal structure of the truncated EBV BFRF1-BFLF2 nuclear egress complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6T3Z
- Type
- protein
- Length
- 217 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nuclear egress protein 2,NUCLEAR egress protein 1
- UniProt
- V5KTU9, A0A2S1N254
- Pockets
- 1 · best druggability 0.34
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear egress protein 2,NUCLEAR egress protein 1 | protein | 217 | 36% helix, 26% strand | V5KTU9, A0A2S1N254 |
Ligands and binding sites
- MLI · Malonate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 52 | 0.34 | 0.78 | 15 | empty |
Compared structures
- 6T3Z · Crystal structure of the truncated EBV BFRF1-BFLF2 nuclear egress 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 V5KTU9
- Every structure of UniProt A0A2S1N254
- Elsewhere: RCSB PDB 6T3Z · PDBe 6T3Z · UniProt V5KTU9 · UniProt A0A2S1N254
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