Research workbench
Cryo-EM structure of MDA5-dsrna in complex with TRIM65 pspry domain (monomer)
Analyse Cryo-EM structure of MDA5-dsrna in complex with TRIM65 pspry domain (monomer) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7JL0
- Type
- protein + RNA
- Length
- 870 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9BYX4, Q6PJ69
- Ligands
- ADP, ALF, ZN, MG
Structure
electron microscopy · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | — | rna | 14 | — | — |
| Y | — | rna | 14 | — | — |
| A | — | protein | 662 | — | Q9BYX4 |
| B | — | protein | 180 | — | Q6PJ69 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- ALF · Tetrafluoroaluminate ion · ligand · chains A
- ZN · Zinc ion · metal · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7JL0 · Cryo-EM structure of MDA5-dsRNA in complex with TRIM65 PSpry domain (Monomer) · the same entry in another collection · chain X against X, TM-score 1.00
- Q6PJ69 · AlphaFold monomer V2.0 prediction for tripartite motif-containing protein 65 (Q6PJ69) · a predicted model of the same protein · chain B against A, TM-score 0.97
- Q9BYX4 · AlphaFold monomer V2.0 prediction for interferon-induced helicase C domain-containing… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q9BYX4
- Every structure of UniProt Q6PJ69
- Elsewhere: RCSB PDB 7JL0 · PDBe 7JL0 · UniProt Q9BYX4 · UniProt Q6PJ69
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