Structure of the extracellular domain of human RAMP2. Determined by X-ray diffraction at 2.05 Å resolution. Released 29 Dec 2010.
Explore 2XVT in 3D Show helices and sheets RCSB PDB PDBe
2XVT 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 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Receptor activity-modifying protein 2 | A, B, C, D, E, F | protein | 94 | HOMO SAPIENS | O60895 (AlphaFold model) |
>2XVT_1 RECEPTOR ACTIVITY-MODIFYING PROTEIN 2 (chains A, B, C, D, E, F) SMTGTPGSEGGTVKNYETAVQFCWNHYKDQMDPIEKDWCDWAMISRPYSTLRDCLEHFAE LFDLGFPNPLAERIIFETHQIHFANCSLVQPTFS
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 3 |
Structure of the Extracellular Domain of Human Ramp2. Quigley, A., Pike, A.C.W., Burgess-Brown, N. et al. To be published.
Other PDB entries of the same protein (UniProt O60895 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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