3AQF: Human CRLR/RAMP2 extracellular complex

Crystal structure of the human CRLR/RAMP2 extracellular complex. Determined by X-ray diffraction at 2.6 Å resolution. Released 2 Nov 2011.

Method
X-ray diffraction
Resolution
2.6 Å
Organism
Homo sapiens
Chains
2
Atoms
1,492
Mol. weight
24.62 kDa
Released
2 Nov 2011

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

Secondary structure: helices and β-sheets

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.

Chain A: 4 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix61-7616
α-helix77-826
α-helix86-10621
α-helix114-12613
Chain B: 5 helices, 12 β-strands
ElementResiduesLengthSheet
α-helix37-5418
α-helix56-583
β-strand64-6521
α-helix66-672
β-strand68-6922
β-strand74-7522
β-strand78-7921
β-strand82-8763
α-helix88-892
β-strand9514
β-strand100-10563
β-strand11113
β-strand11315
β-strand12015
β-strand12313
β-strand12814
α-helix129-1313

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Receptor activity-modifying protein 2Aprotein91Homo sapiensO60895 (AlphaFold model)
Calcitonin gene-related peptide type 1 receptorBprotein121Homo sapiensQ16602 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3AQF_1 Receptor activity-modifying protein 2 (chains A)
GSSGSSGGTVKNYETAVQFCWNHYKDQMDPIEKDWCDWAMISRPYSTLRDCLEHFAELFD
LGFPNPLAERIIFETHQIHFANCSLVQPTFS
Sequence of entity 2 (B), FASTA
>3AQF_2 Calcitonin gene-related peptide type 1 receptor (chains B)
GSSGSSGELEESPEDSIQLGVTRNKIMTAQYECYQKIMQDPIQQAEGVYCNRTWDGWLCW
NDVAAGTESMQLCPDYFQDFDPSEKVTKICDQDGNWFRHPASNRTWTNYTQCNVNTHEKV
K

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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