2JNU: RGS domain of human RGS14

Solution structure of the RGS domain of human RGS14. Determined by solution NMR. Released 27 Feb 2007.

Method: Solution NMR
Organism: Homo sapiens
Chains: 1
Atoms: 1,119
Mol. weight: 17.72 kDa
Released: 27 Feb 2007

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

Secondary structure: helices and β-sheets

2JNU contains 10 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: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	8-12	5
α-helix	15-20	6
α-helix	22-31	10
α-helix	39-52	14
α-helix	58-68	11
α-helix	69-73	5
α-helix	91-95	5
α-helix	103-114	12
α-helix	117-121	5
α-helix	127-131	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Regulator of G-protein signaling 14	A	protein	154	Homo sapiens	O43566 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2JNU_1 Regulator of G-protein signaling 14 (chains A)
SMTEEQPVASWALSFERLLQDPLGLAYFTEFLKKEFSAENVTFWKACERFQQIPASDTQQ
LAQEARNIYQEFLSSQALSPVNIDRQAWLGEEVLAEPRPDMFRAQQLQIFNLMKFDSYAR
FVKSPLYRECLLAEAEGRPLREPGSSRLGSPDAT

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 O43566 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2OM2 2.2 Å, Crystal Structure Of Human G[alpha]i1 Bound To The Goloco Motif Of Rgs14
3ONW 2.38 Å, Structure of a G-alpha-i1 mutant with enhanced affinity for the RGS14 GoLoco motif.
3QI2 2.8 Å, A Galpha P-loop mutation prevents transition to the activated state: G42R bound to RGS14…
2XNS 3.41 Å, Crystal Structure Of Human G alpha i1 Bound To A Designed Helical Peptide Derived From…

Browse structure collections

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