Crystal structure of the human CRLR/RAMP2 extracellular complex. Determined by X-ray diffraction at 2.6 Å resolution. Released 2 Nov 2011.
Explore 3AQF in 3D Show helices and sheets RCSB PDB PDBe
3AQF contains 9 α-helices and 12 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 61-76 | 16 | |
| α-helix | 77-82 | 6 | |
| α-helix | 86-106 | 21 | |
| α-helix | 114-126 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 37-54 | 18 | |
| α-helix | 56-58 | 3 | |
| β-strand | 64-65 | 2 | 1 |
| α-helix | 66-67 | 2 | |
| β-strand | 68-69 | 2 | 2 |
| β-strand | 74-75 | 2 | 2 |
| β-strand | 78-79 | 2 | 1 |
| β-strand | 82-87 | 6 | 3 |
| α-helix | 88-89 | 2 | |
| β-strand | 95 | 1 | 4 |
| β-strand | 100-105 | 6 | 3 |
| β-strand | 111 | 1 | 3 |
| β-strand | 113 | 1 | 5 |
| β-strand | 120 | 1 | 5 |
| β-strand | 123 | 1 | 3 |
| β-strand | 128 | 1 | 4 |
| α-helix | 129-131 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Receptor activity-modifying protein 2 | A | protein | 91 | Homo sapiens | O60895 (AlphaFold model) |
| Calcitonin gene-related peptide type 1 receptor | B | protein | 121 | Homo sapiens | Q16602 (AlphaFold model) |
>3AQF_1 Receptor activity-modifying protein 2 (chains A) GSSGSSGGTVKNYETAVQFCWNHYKDQMDPIEKDWCDWAMISRPYSTLRDCLEHFAELFD LGFPNPLAERIIFETHQIHFANCSLVQPTFS
>3AQF_2 Calcitonin gene-related peptide type 1 receptor (chains B) GSSGSSGELEESPEDSIQLGVTRNKIMTAQYECYQKIMQDPIQQAEGVYCNRTWDGWLCW NDVAAGTESMQLCPDYFQDFDPSEKVTKICDQDGNWFRHPASNRTWTNYTQCNVNTHEKV K
Structural basis for extracellular interactions between calcitonin receptor-like receptor and receptor activity-modifying protein 2 for adrenomedullin-specific binding. Kusano, S., Kukimoto-Niino, M., Hino, N. et al. Protein Sci (2012) 21:199-210. DOI 10.1002/pro.2003 · PubMed
Other PDB entries of the same protein (UniProt O60895 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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