Research workbench
AlphaFold monomer V2.0 prediction for atrial natriuretic peptide receptor 1 (P16066)
Analyse AlphaFold monomer V2.0 prediction for atrial natriuretic peptide receptor 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P16066
- Type
- protein
- Length
- 1,061 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x16b7713AB0A29210E6F789787Aee3C4a08446102
- UniProt
- P16066
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1061 | — | P16066 |
Compared structures
- 9BCQ · Extracellular domain of GC-A bound to ANP · an experimental structure of the same protein · chain A against B, TM-score 0.40
- 9BCL · Extracellular domain of apo GC-A, state 1 · an experimental structure of the same protein · chain A against B, TM-score 0.40
- 9BCN · Extracellular domain of apo GC-A, state 2 · an experimental structure of the same protein · chain A against A, TM-score 0.40
- 8TG9 · Complex of NPR1 ectodomain with ANP plus an allosteric activating antibody, REGN5381 · an experimental structure of the same protein · chain A against A, TM-score 0.40
- 8TGA · Complex of NPR1 ectodomain and REGN5381 Fab in an active-like state with no ANP bound · an experimental structure of the same protein · chain A against B, TM-score 0.40
- 9BCO · Intracellular domain of apo GC-A · an experimental structure of the same protein · chain A against B, TM-score 0.33
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 P16066
- Elsewhere: UniProt P16066 · AlphaFold DB P16066
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.