2AF0: Regulator of G-Protein Signaling Domain of RGS2

Structure of the Regulator of G-Protein Signaling Domain of RGS2. Determined by X-ray diffraction at 2.3 Å resolution. Released 2 Aug 2005.

Method
X-ray diffraction
Resolution
2.3 Å
Organism
Homo sapiens
Chains
1
Atoms
1,166
Mol. weight
16.99 kDa
Released
2 Aug 2005

Explore 2AF0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2AF0 contains 14 α-helices and 0 β-strands across 1 chain. 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: 14 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix62-698
α-helix72-732
α-helix74-796
α-helix84-896
α-helix91-10313
α-helix108-12013
α-helix125-13511
α-helix136-1405
α-helix152-16110
α-helix162-1643
α-helix171-18010
α-helix181-1855
α-helix186-1916
α-helix193-1997

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Regulator of G-protein signaling 2Aprotein146Homo sapiensP41220 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2AF0_1 Regulator of G-protein signaling 2 (chains A)
ADLGTENLYFQSMKPSPEEAQLWSEAFDELLASKYGLAAFRAFLKSEFCEENIEFWLACE
DFKKTKSPQKLSSKARKIYTDFIEKEAPKEINIDFQTKTLIAQNIQEATSGCFTTAQKRV
YSLMENNSYPRFLESEFYQDLCKKPQ

Primary citation

Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits. Soundararajan, M., Willard, F.S., Kimple, A.J. et al. Proc Natl Acad Sci U S A (2008) 105:6457-6462. DOI 10.1073/pnas.0801508105 · PubMed

Other PDB entries of the same protein (UniProt P41220 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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