Research workbench
West nile virus envelope protein diii in complex with neutralizing E16 antibody Fab
Analyse West nile virus envelope protein diii in complex with neutralizing E16 antibody… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZTX
- Type
- protein
- Length
- 532 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Envelope protein; Heavy chain of E16 antibody; Light chain of E16 antibody
- UniProt
- Q91KZ4
- Pockets
- 7 · best druggability 0.68
Structure
x-ray diffraction · 3 distinct chains · 5% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Envelope protein | protein | 101 | 3% helix, 54% strand | Q91KZ4 |
| H | Heavy chain of E16 antibody | protein | 219 | 5% helix, 55% strand | — |
| L | Light chain of E16 antibody | protein | 212 | 6% helix, 50% strand | — |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 775 | 0.68 | 0.76 | 62 | empty |
| 2 | 55 | 0.43 | 0.83 | 19 | empty |
| 3 | 124 | 0.39 | 0.75 | 25 | empty |
| 4 | 74 | 0.33 | 0.75 | 24 | empty |
| 5 | 62 | 0.31 | 0.75 | 22 | empty |
Interfaces
3 interfaces between chains.
- H–L · 1868 Ų buried · 14 hydrogen bonds · protein-protein
- E–H · 603 Ų buried · 19 hydrogen bonds · protein-protein
- E–L · 299 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 1ZTX · West Nile Virus Envelope Protein DIII in complex with neutralizing E16 antibody Fab · 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 Q91KZ4
- Elsewhere: RCSB PDB 1ZTX · PDBe 1ZTX · UniProt Q91KZ4
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