2I59: RGS10

Solution structure of RGS10. Determined by solution NMR. Released 31 Oct 2006.

Method: Solution NMR
Organism: Homo sapiens
Chains: 1
Atoms: 1,158
Mol. weight: 16.51 kDa
Released: 31 Oct 2006

Explore 2I59 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2I59 contains 11 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: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	5-11	7
α-helix	15-20	6
α-helix	22-35	14
α-helix	38-52	15
α-helix	56-66	11
α-helix	67-71	5
α-helix	75-77	3
α-helix	89-92	4
α-helix	97-110	14
α-helix	111-115	5
α-helix	116-119	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Regulator of G-protein signaling 10	A	protein	138	Homo sapiens	O43665 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2I59_1 Regulator of G-protein signaling 10 (chains A)
SMQSLKSTAKWAASLENLLEDPEGVKRFREFLKKEFSEENVLFWLACEDFKKMQDKTQMQ
EKAKEIYMTFLSSKASSQVNVEGQSRLNEKILEEPHPLMFQKLQDQIFNLMKYDSYSRFL
KSDLFLKHKRTEEEEEDL

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 O43665 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2IHB 2.71 Å, Crystal structure of the heterodimeric complex of human RGS10 and activated Gi alpha 3
2DLR Solution structure of the RGS domain of human Regulator of G-protein signaling 10

Browse structure collections

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