Research workbench
Crystal structure of three main domains of nonstructural protein 3 from coronavirus
Analyse Crystal structure of three main domains of nonstructural protein 3 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LN0
- Type
- protein
- Length
- 425 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Non-structural protein 3
- UniProt
- A0A222YV61
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Non-structural protein 3 | protein | 425 | 31% helix, 27% strand | A0A222YV61 |
Ligands and binding sites
- ZN · Zinc ion · metal · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 199 | 0.50 | 0.76 | 32 | empty |
| 2 | 58 | 0.44 | 0.83 | 17 | empty |
| 3 | 59 | 0.29 | 0.74 | 16 | empty |
Compared structures
- 6LN0 · Crystal structure of three main domains of nonstructural protein 3 from Coronavirus · 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 A0A222YV61
- Elsewhere: RCSB PDB 6LN0 · PDBe 6LN0 · UniProt A0A222YV61
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