Research workbench
Cryoem structure of full-length zikv NS5-HSTAT2 complex
Analyse Cryoem structure of full-length zikv NS5-HSTAT2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6WCZ
- Type
- protein
- Length
- 1,231 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Signal transducer and activator of transcription 2; Non-structural protein 5
- UniProt
- P52630, A0A2R4LVT4
- Ligands
- ZN
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 2 distinct chains · 40% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Signal transducer and activator of transcription 2 | protein | 350 | 46% helix, 12% strand | P52630 |
| B | Non-structural protein 5 | protein | 881 | 38% helix, 10% strand | A0A2R4LVT4 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 841 | 0.83 | 0.85 | 98 | empty |
| 2 | 1185 | 0.78 | 0.80 | 101 | empty |
| 3 | 109 | 0.76 | 0.95 | 25 | empty |
| 4 | 106 | 0.75 | 0.95 | 23 | empty |
| 5 | 62 | 0.70 | 0.96 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1436 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 6WCZ · CryoEM structure of full-length ZIKV NS5-hSTAT2 complex · the same entry in another collection · chain A against A, TM-score 1.00
- P52630 · AlphaFold monomer V2.0 prediction for signal transducer and activator of transcription 2… · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P52630
- Every structure of UniProt A0A2R4LVT4
- Elsewhere: RCSB PDB 6WCZ · PDBe 6WCZ · UniProt P52630 · UniProt A0A2R4LVT4
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