Research workbench
The crystal structure of zika virus NS3 helicase domain
Analyse The crystal structure of zika virus NS3 helicase domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MH3
- Type
- protein
- Length
- 435 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Zika virus NS3 helicase domain
- EC
- 3.6.4.13
- UniProt
- Q32ZE1
- Ligands
- PO4
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Zika virus NS3 helicase domain (EC 3.6.4.13) | protein | 435 | 33% helix, 19% strand | Q32ZE1 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 995 | 0.80 | 0.81 | 72 | EDO, PO4, MPD |
| 2 | 206 | 0.59 | 0.81 | 37 | PO4 |
| 3 | 54 | 0.31 | 0.76 | 16 | empty |
Compared structures
- 6MH3 · The crystal structure of Zika virus NS3 helicase domain · 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 Q32ZE1
- Elsewhere: RCSB PDB 6MH3 · PDBe 6MH3 · UniProt Q32ZE1
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