Research workbench
Cryo-EM structure of rhinovirus-B5 complexed to antiviral obr-5-340
Analyse Cryo-EM structure of rhinovirus-B5 complexed to antiviral obr-5-340 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SK5
- Type
- protein
- Length
- 795 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q80SQ3, B9V433, Q7T659
- Ligands
- LGQ
Structure
electron microscopy · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D | — | protein | 40 | — | Q80SQ3 |
| B | — | protein | 252 | — | B9V433 |
| A | — | protein | 273 | — | Q7T659 |
| C | — | protein | 230 | — | B9V433 |
Ligands and binding sites
- LGQ · 6-phenyl-~{N}3-[4-(trifluoromethyl)phenyl]-1~{H}-pyrazolo[3,4-d]pyrimidine-3,4-diamine · ligand · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6SK5 · Cryo-EM structure of rhinovirus-B5 complexed to antiviral OBR-5-340 · the same entry in another collection · chain D against D, 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 Q80SQ3
- Every structure of UniProt B9V433
- Every structure of UniProt Q7T659
- Elsewhere: RCSB PDB 6SK5 · PDBe 6SK5 · UniProt Q80SQ3 · UniProt B9V433 · UniProt Q7T659
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.