Research workbench
Zika virus E protein complexed with a neutralizing antibody Z23-Fab
Analyse Zika virus E protein complexed with a neutralizing antibody Z23-Fab in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5GZR
- Type
- protein
- Length
- 2,601 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Structural protein E; Strutural protein M; Z23 Fab heavy chain; Z23 Fab light chain
- UniProt
- A0A024B7W1
- Pockets
- 8 · best druggability 0.47
Structure
electron microscopy · 4 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Structural protein E | protein | 504 | 0% helix, 0% strand | A0A024B7W1 |
| D, E, F | Strutural protein M | protein | 75 | 0% helix, 0% strand | A0A024B7W1 |
| H, M | Z23 Fab heavy chain | protein | 221 | 0% helix, 0% strand | — |
| L, N | Z23 Fab light chain | protein | 211 | 0% helix, 0% strand | — |
Pockets
8 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 198 | 0.47 | 0.73 | 44 | empty |
| 2 | 117 | 0.39 | 0.73 | 31 | empty |
| 3 | 96 | 0.36 | 0.72 | 24 | empty |
| 4 | 89 | 0.35 | 0.73 | 26 | empty |
| 5 | 78 | 0.32 | 0.72 | 28 | empty |
Interfaces
11 interfaces between chains.
- M–N · 319 Ų buried · 0 hydrogen bonds · protein-protein
- H–L · 318 Ų buried · 0 hydrogen bonds · protein-protein
- C–F · 302 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 295 Ų buried · 0 hydrogen bonds · protein-protein
- B–E · 292 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 5GZR · Zika virus E protein complexed with a neutralizing antibody Z23-Fab · 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 A0A024B7W1
- Elsewhere: RCSB PDB 5GZR · PDBe 5GZR · UniProt A0A024B7W1
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