Research workbench
Crystal structure of the ectodomain complex of the cgrp receptor, a class-B GPCR, reveals the site of drug antagonism
Analyse Crystal structure of the ectodomain complex of the cgrp receptor, a class-B… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3N7R
- Type
- protein
- Length
- 345 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q16602, O60894
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 91 | — | Q16602 |
| B | — | protein | 92 | — | Q16602 |
| C | — | protein | 82 | — | O60894 |
| D | — | protein | 80 | — | O60894 |
Compared structures
- 3N7R · Crystal structure of the ectodomain complex of the CGRP receptor, a Class-B GPCR, reveals… · the same entry in another collection · chain D against D, TM-score 1.00
- O60894 · AlphaFold monomer V2.0 prediction for receptor activity-modifying protein 1 (O60894) · a predicted model of the same protein · chain D against A, TM-score 0.99
- Q16602 · AlphaFold monomer V2.0 prediction for calcitonin gene-related peptide type 1 receptor… · a predicted model of the same protein · chain B against A, TM-score 0.97
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 Q16602
- Every structure of UniProt O60894
- Elsewhere: RCSB PDB 3N7R · PDBe 3N7R · UniProt Q16602 · UniProt O60894
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