Research workbench
AlphaFold monomer V2.0 prediction for apelin receptor early endogenous ligand (P0DMC3)
Analyse AlphaFold monomer V2.0 prediction for apelin receptor early endogenous ligand… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0DMC3
- Type
- protein
- Length
- 54 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7D876F364ae377f396cf395997491B94DB9a3335
- UniProt
- P0DMC3
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 54 | — | P0DMC3 |
Compared structures
- 7W0P · Cryo-EM structure of a GPCR-gi complex with peptide · an experimental structure of the same protein · chain A against D, TM-score 0.16
- 7W0P · Cryo-EM structure of a GPCR-Gi complex with peptide · an experimental structure of the same protein · chain A against D, TM-score 0.16
- 7W0N · Cryo-EM structure of a dimeric GPCR-gi complex with peptide · an experimental structure of the same protein · chain A against E, TM-score 0.16
- 7W0N · Cryo-EM structure of a dimeric GPCR-Gi complex with peptide · an experimental structure of the same protein · chain A against E, TM-score 0.16
- 7W0O · Cryo-EM structure of a monomeric GPCR-Gi complex with peptide · an experimental structure of the same protein · chain A against D, TM-score 0.12
- 7W0O · Cryo-EM structure of a monomeric GPCR-gi complex with peptide · an experimental structure of the same protein · chain A against D, TM-score 0.12
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 P0DMC3
- Elsewhere: UniProt P0DMC3 · AlphaFold DB P0DMC3
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