› 3aqe

X-ray diffraction
2Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo trimer
Assembly name:
PDBe Complex ID:
PDB-CPX-130167 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Receptor activity-modifying protein 2 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 91 amino acids
Theoretical weight: 10.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli cell-free system
UniProt:
  • Canonical: O60895 (Residues: 56-139; Coverage: 63%)
Gene name: RAMP2
Sequence domains: Receptor activity modifying family
Structure domains: Receptor activity modifying family

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 12 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P212121
Unit cell:
a: 59.571Å b: 89.729Å c: 91.998Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.23 0.276
Expression system: Escherichia coli cell-free system

Quick links

Citations

8 review citations

Receptor Activity-Modifying Proteins (RAMPs): New Insights and Roles.
Hay et al. (2016)
7 more

4 mentions without citation

RAMPs as allosteric modulators of the calcitonin and calcitonin-like class B G protein-coupled receptors.
Pioszak et al. (2020)
3 more