Research workbench
Crystal structure of catalytic domain of japanese encephalitis virus NS3 HELICASE/NUCLEOSIDE triphosphatase at a resolution 1.8
Analyse Crystal structure of catalytic domain of japanese encephalitis virus NS3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Z83
- Type
- protein
- Length
- 426 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HELICASE/NUCLEOSIDE triphosphatase
- UniProt
- Q5NT71
- Pockets
- 2 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | HELICASE/NUCLEOSIDE triphosphatase | protein | 426 | 34% helix, 18% strand | Q5NT71 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1136 | 0.80 | 0.81 | 104 | empty |
| 2 | 64 | 0.30 | 0.74 | 17 | empty |
Compared structures
- 2Z83 · Crystal Structure of Catalytic Domain of Japanese Encephalitis Virus NS3… · 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 Q5NT71
- Elsewhere: RCSB PDB 2Z83 · PDBe 2Z83 · UniProt Q5NT71
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