Research workbench
Crystal structure of the zika virus NS3 helicase complex with amppnp
Analyse Crystal structure of the zika virus NS3 helicase complex with amppnp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5Y4Z
- Type
- protein
- Length
- 440 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NS3 helicase
- EC
- 3.4.21.91, 3.6.1.15, 3.6.4.13
- UniProt
- Q32ZE1
- Ligands
- ANP, 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 | NS3 helicase (EC 3.4.21.91, 3.6.1.15, 3.6.4.13) | protein | 440 | 34% helix, 19% strand | Q32ZE1 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
- MN · Manganese (II) ion · metal · chains A
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 | 1148 | 0.81 | 0.82 | 101 | empty |
| 2 | 204 | 0.61 | 0.82 | 36 | ANP, MN |
Compared structures
- 5Y4Z · Crystal structure of the Zika virus NS3 helicase complex with AMPPNP · 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 5Y4Z · PDBe 5Y4Z · UniProt Q32ZE1
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