Crystal structure of the extracellular domain of human RAMP2. Determined by X-ray diffraction at 2.0 Å resolution. Released 9 Nov 2011.
Explore 3AQE in 3D Show helices and sheets RCSB PDB PDBe
3AQE contains 30 α-helices and 0 β-strands across 6 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 | 114-123 | 10 | |
| α-helix | 124-128 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 61-76 | 16 | |
| α-helix | 77-82 | 6 | |
| α-helix | 90-106 | 17 | |
| α-helix | 114-123 | 10 | |
| α-helix | 124-128 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Receptor activity-modifying protein 2 | A, B, C, D, E, F | protein | 91 | Homo sapiens | O60895 (AlphaFold model) |
>3AQE_1 Receptor activity-modifying protein 2 (chains A, B, C, D, E, F) GSSGSSGGTVKNYETAVQFCWNHYKDQMDPIEKDWCDWAMISRPYSTLRDCLEHFAELFD LGFPNPLAERIIFETHQIHFANCSLVQPTFS
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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