Research workbench
Crystal structure of epstein-barr virus GP42 protein
Analyse Crystal structure of epstein-barr virus GP42 protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FD4
- Type
- protein
- Length
- 287 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycoprotein GP42
- UniProt
- P03205
- Pockets
- 2 · best druggability 0.27
Structure
x-ray diffraction · 2 distinct chains · 10% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycoprotein GP42 | protein | 140 | 10% helix, 28% strand | P03205 |
| B | Glycoprotein GP42 | protein | 147 | 10% helix, 24% strand | P03205 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 60 | 0.27 | 0.73 | 15 | empty |
| 2 | 53 | 0.27 | 0.73 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 815 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 3FD4 · Crystal Structure of Epstein-Barr virus gp42 protein · 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 P03205
- Elsewhere: RCSB PDB 3FD4 · PDBe 3FD4 · UniProt P03205
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