2XVT: Extracellular domain of human RAMP2

Structure of the extracellular domain of human RAMP2. Determined by X-ray diffraction at 2.05 Å resolution. Released 29 Dec 2010.

Method
X-ray diffraction
Resolution
2.05 Å
Organism
HOMO SAPIENS
Chains
6
Atoms
4,177
Mol. weight
65.36 kDa
Ligands
CA
Released
29 Dec 2010

Explore 2XVT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chains A, B, 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

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Receptor activity-modifying protein 2A, B, C, D, E, Fprotein94HOMO SAPIENSO60895 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>2XVT_1 RECEPTOR ACTIVITY-MODIFYING PROTEIN 2 (chains A, B, C, D, E, F)
SMTGTPGSEGGTVKNYETAVQFCWNHYKDQMDPIEKDWCDWAMISRPYSTLRDCLEHFAE
LFDLGFPNPLAERIIFETHQIHFANCSLVQPTFS

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa3

Primary citation

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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