Research workbench
AlphaFold monomer V2.0 prediction for G-protein coupled estrogen receptor 1 (Q99527)
Analyse AlphaFold monomer V2.0 prediction for G-protein coupled estrogen receptor 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q99527
- Type
- protein
- Length
- 375 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5e58272ea25a05e06901A2eAe9f63939b344e0c6
- UniProt
- Q99527
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 375 | — | Q99527 |
Compared structures
- 8XOJ · Cryo-EM structure of GPR30-Gq complex structure in the presence of G-1 · an experimental structure of the same protein · chain A against R, TM-score 0.64
- 8XOH · Cryo-EM structure of GPR30-Gq complex structure in the presence of E2 · an experimental structure of the same protein · chain A against R, TM-score 0.64
- 8XOI · Cryo-EM structure of GPR30-Gq complex structure in the presence of fulvestrant · an experimental structure of the same protein · chain A against R, TM-score 0.64
- 8XOF · Cryo-EM structure of Lys05 bound GPR30-Gq complex structure · an experimental structure of the same protein · chain A against R, TM-score 0.63
- 8XOG · Cryo-EM structure of apo-GPR30-Gq complex structure · an experimental structure of the same protein · chain A against R, TM-score 0.63
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 Q99527
- Elsewhere: UniProt Q99527 · AlphaFold DB Q99527
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