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Crystal structure of the west nile virus envelope glycoprotein in complex with the E53 antibody Fab
Analyse Crystal structure of the west nile virus envelope glycoprotein in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3I50
- Type
- protein
- Length
- 692 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Envelope glycoprotein; Murine kappa light chain of E53 monoclonal antibody Fab; Murine…
- UniProt
- Q91R02
- Pockets
- 9 · best druggability 0.69
Structure
x-ray diffraction · 3 distinct chains · 6% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Envelope glycoprotein | protein | 273 | 10% helix, 42% strand | Q91R02 |
| L | Murine kappa light chain of E53 monoclonal antibody Fab | protein | 207 | 3% helix, 39% strand | — |
| H | Murine heavy chain (IGG3) of E53 monoclonal antibody Fab | protein | 212 | 3% helix, 43% strand | — |
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 106 | 0.69 | 0.91 | 22 | empty |
| 2 | 176 | 0.67 | 0.87 | 35 | empty |
| 3 | 648 | 0.64 | 0.75 | 60 | empty |
| 4 | 63 | 0.52 | 0.86 | 14 | empty |
| 5 | 71 | 0.45 | 0.82 | 22 | empty |
Interfaces
3 interfaces between chains.
- L–H · 1723 Ų buried · 14 hydrogen bonds · protein-protein
- E–H · 552 Ų buried · 7 hydrogen bonds · protein-protein
- E–L · 74 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 3I50 · Crystal structure of the West Nile Virus envelope glycoprotein in complex with the E53… · the same entry in another collection · chain E against E, 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 Q91R02
- Elsewhere: RCSB PDB 3I50 · PDBe 3I50 · UniProt Q91R02
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