3AQE: Extracellular domain of human RAMP2

Crystal structure of the extracellular domain of human RAMP2. Determined by X-ray diffraction at 2.0 Å resolution. Released 9 Nov 2011.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
6
Atoms
4,091
Mol. weight
63.49 kDa
Released
9 Nov 2011

Explore 3AQE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chains A, C, D, E and F: 5 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix61-7616
α-helix77-826
α-helix86-10621
α-helix114-12310
α-helix124-1285
Chain B: 5 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix61-7616
α-helix77-826
α-helix90-10617
α-helix114-12310
α-helix124-1285

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Receptor activity-modifying protein 2A, B, C, D, E, Fprotein91Homo sapiensO60895 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>3AQE_1 Receptor activity-modifying protein 2 (chains A, B, C, D, E, F)
GSSGSSGGTVKNYETAVQFCWNHYKDQMDPIEKDWCDWAMISRPYSTLRDCLEHFAELFD
LGFPNPLAERIIFETHQIHFANCSLVQPTFS

Primary citation

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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