Research workbench
SARS coronavirus-unique domain (sud): three-domain molecular architecture in solution and RNA binding. I: structure of the sud-M domain of sud-mc
Analyse SARS coronavirus-unique domain (sud): three-domain molecular architecture in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KQV
- Type
- protein
- Length
- 129 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Non-structural protein 3
- UniProt
- P0C6U8
- Pockets
- 2 · best druggability 0.48
Structure
solution nmr · 1 distinct chain · 37% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Non-structural protein 3 | protein | 129 | 37% helix, 13% strand | P0C6U8 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 145 | 0.48 | 0.77 | 24 | empty |
| 2 | 58 | 0.35 | 0.78 | 16 | empty |
Compared structures
- 2KQV · SARS coronavirus-unique domain (SUD): Three-domain molecular architecture in solution and… · 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 P0C6U8
- Elsewhere: RCSB PDB 2KQV · PDBe 2KQV · UniProt P0C6U8
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