Research workbench
Crystal structure of the human CRLR/RAMP2 extracellular complex
Analyse Crystal structure of the human CRLR/RAMP2 extracellular complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3AQF
- Type
- protein
- Length
- 176 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor activity-modifying protein 2; Calcitonin gene-related peptide type 1 receptor
- UniProt
- O60895, Q16602
- Pockets
- 1 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor activity-modifying protein 2 | protein | 79 | 71% helix, 0% strand | O60895 |
| B | Calcitonin gene-related peptide type 1 receptor | protein | 97 | 22% helix, 27% strand | Q16602 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 219 | 0.46 | 0.74 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 980 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide, 5 modified (disulfide, engineered).
Compared structures
- 3AQF · Crystal structure of the human CRLR/RAMP2 extracellular complex · the same entry in another collection · chain A against A, TM-score 1.00
- O60895 · AlphaFold monomer V2.0 prediction for receptor activity-modifying protein 2 (O60895) · a predicted model of the same protein · chain A against A, TM-score 0.92
- 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 0.88
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 O60895
- Every structure of UniProt Q16602
- Elsewhere: RCSB PDB 3AQF · PDBe 3AQF · UniProt O60895 · UniProt Q16602
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