Research workbench
Zika virus NS3 helicase in complex with ATP
Analyse Zika virus NS3 helicase in complex with ATP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5GJC
- Type
- protein
- Length
- 429 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NS3 helicase
- UniProt
- A0A142DS38
- Ligands
- ATP, MN
- Pockets
- 5 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NS3 helicase | protein | 429 | 33% helix, 19% strand | A0A142DS38 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1138 | 0.82 | 0.83 | 104 | empty |
| 2 | 92 | 0.58 | 0.87 | 23 | MN, ATP |
| 3 | 81 | 0.33 | 0.75 | 17 | empty |
| 4 | 53 | 0.32 | 0.77 | 15 | empty |
| 5 | 66 | 0.32 | 0.75 | 19 | empty |
Compared structures
- 5GJC · Zika virus NS3 helicase in complex with ATP · 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 A0A142DS38
- Elsewhere: RCSB PDB 5GJC · PDBe 5GJC · UniProt A0A142DS38
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