Research workbench
Crystal structure of the zika virus NS3 helicase (ADP-MN2+ complex, form 1)
Analyse Crystal structure of the zika virus NS3 helicase (ADP-MN2+ complex, form 1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ADX
- Type
- protein
- Length
- 430 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine protease NS3
- EC
- 3.4.21.91, 3.6.1.15, 3.6.4.13
- UniProt
- Q32ZE1
- Ligands
- ADP, MN
- Pockets
- 2 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine protease NS3 (EC 3.4.21.91, 3.6.1.15, 3.6.4.13) | protein | 430 | 34% helix, 19% strand | Q32ZE1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 978 | 0.81 | 0.83 | 91 | empty |
| 2 | 121 | 0.59 | 0.86 | 23 | ADP, MN |
Compared structures
- 6ADX · Crystal structure of the Zika virus NS3 helicase (ADP-Mn2+ complex, form 1) · 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 6ADX · PDBe 6ADX · UniProt Q32ZE1
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