Research workbench
AlphaFold monomer V2.0 prediction for low-density lipoprotein receptor class a domain-containing protein 3 (Q86YD5)
Analyse AlphaFold monomer V2.0 prediction for low-density lipoprotein receptor class a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q86YD5
- Type
- protein
- Length
- 345 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x46EfCa788d03A3e879DAcDb96552AB8Bbc7e20b3
- UniProt
- Q86YD5
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 345 | — | Q86YD5 |
Compared structures
- 7FFF · Structure of Venezuelan equine encephalitis virus with the receptor LDLRAD3 · an experimental structure of the same protein · chain A against E, TM-score 0.11
- 7FFL · Cryo-EM structure of VEEV VLP-LDLRAD3-D1 complex at the 2-fold axes · an experimental structure of the same protein · chain A against E, TM-score 0.11
- 7FFN · Cryo-EM structure of veev vlp-LDLRAD3-D1 complex at the 5-fold axes · an experimental structure of the same protein · chain A against M, TM-score 0.11
- 7FFN · Cryo-EM structure of VEEV VLP-LDLRAD3-D1 complex at the 5-fold axes · an experimental structure of the same protein · chain A against M, TM-score 0.11
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 Q86YD5
- Elsewhere: UniProt Q86YD5 · AlphaFold DB Q86YD5
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