Alignments and Trees
Segment and residue customized sequence alignments and phylogenetic trees.
Structure Determination Resource
Construct design tool and suggested thermostabilizing mutations.
Homology Models
Multiple template homology models for the whole GPCRome.
Residue Plots
Customizable helix and snake plots for GPCR's, G-proteins and B-arrestins.
GPCRdb contains reference data, interactive visualisation and experiment design tools for G protein-coupled receptors (GPCRs). GPCRdb curates sequence alignments, structures and receptor mutations from literature. Interactive diagrams visualise receptor residues (e.g. snakeplot and helix box plot) and relationships (e.g phylogenetic trees). See the GPCRdb graphical overview, video, articles or documentation.
GPCRdb is developed by the David Gloriam group, integrates data from the large GPCR community and maintains an active collaboration with the Guide To Pharmacology (IUPHAR), GPCRmd and ERNEST. If you use the GPCRdb, please remember to cite us.
GPCRdb statistics
- Human proteins: 424
- Species orthologs: 43,091
- Structures: GPCRs: 537, G proteins: 220
- Structure models: GPCRs: 1014, GPCR-G protein complexes: 3074
- Refined GPCR structures: 471
- Genetic variants: 69,605
- Drugs: 1,789
- Ligands: 199,277
- Ligand site mutations: 34,687
- Ligand interactions: 27,302
Latest release
April 14, 2021- Release of structure comparison resources (see preprint):
- Improved complex homology modeling workflow:
- Utilizing alternative backbone templates and rotamer switching.
- For GPCR-G protein complex structures, the G protein is now refined as well.
- Updated GPCR and G protein structures.
- Updated GPCR homology and refined structure models.
- Updated references.
- Minor bug and performance fixes.