MolNFT v1 · #178766 · protein + RNA
Cryo-EM structure of rig-I:DSRNA in complex with riplet pryspry domain (monomer)
7JL1: “Cryo-EM structure of rig-I:DSRNA in complex with riplet pryspry domain (monomer)”. Electron microscopy, 4 ligands (ADP, ALF, MG). MolNFT v1 #178766 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7JL1
- Type
- protein + RNA
- Length
- 855 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O95786, Q8IUD6
- Ligands
- ADP, ALF, MG, ZN
Structure
electron microscopy · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 656 | — | O95786 |
| X | — | rna | 14 | — | — |
| Y | — | rna | 14 | — | — |
| B | — | protein | 171 | — | Q8IUD6 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- ALF · Tetrafluoroaluminate ion · ligand · chains A
- MG · Magnesium ion · metal · chains A
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7JL1 · Cryo-EM structure of RIG-I:dsRNA in complex with RIPLET PrySpry domain (monomer) · the same entry in another collection · chain A against A, TM-score 1.00
- Q8IUD6 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RNF135 (Q8IUD6) · a predicted model of the same protein · chain B against A, TM-score 0.98
- O95786 · AlphaFold monomer V2.0 prediction for antiviral innate immune response receptor rig-I… · a predicted model of the same protein · chain A against A, TM-score 0.90
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 O95786
- Every structure of UniProt Q8IUD6
- Elsewhere: RCSB PDB 7JL1 · PDBe 7JL1 · UniProt O95786 · UniProt Q8IUD6
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