› 2ik8

X-ray diffraction
2.71Å resolution

Crystal structure of the heterodimeric complex of human RGS16 and activated Gi alpha 1

Released:
DOI: 10.2210/pdb2ik8/pdb
PDB entry 2ik8 coloured by chain, front view.
PDB entry 2ik8 coloured by chain, side view.
PDB entry 2ik8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits.
Soundararajan M, Willard FS, Kimple AJ, Turnbull AP, Ball LJ, Schoch GA, Gileadi C, Fedorov OY, Dowler EF, Higman VA, Hutsell SQ, Sundström M, Doyle DA, Siderovski DP
Proc Natl Acad Sci U S A 105 6457-62 (2008)
PMID: 18434541

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127494 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Guanine nucleotide-binding protein G(i) subunit alpha-1 Chains: A, C
Molecule details ›
Chains: A, C
Length: 324 amino acids
Theoretical weight: 37.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P63096 (Residues: 31-354; Coverage: 92%)
Gene name: GNAI1
Sequence domains: G-protein alpha subunit
Structure domains:
Regulator of G-protein signaling 16 Chains: B, D
Molecule details ›
Chains: B, D
Length: 140 amino acids
Theoretical weight: 15.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O15492 (Residues: 53-190; Coverage: 68%)
Gene names: RGS16, RGSR
Sequence domains: Regulator of G protein signaling domain
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand ALF 2 x ALF
Ligand MG 2 x MG
Ligand SO4 8 x SO4
Ligand GDP 2 x GDP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 82.656Å b: 104.312Å c: 124.048Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.235 0.232 0.291
Expression system: Escherichia coli

Quick links

Citations

22 review citations

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Jockers et al. (2016)
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13 mentions without citation

Discovery of new GPCR biology: one receptor structure at a time.
Hanson et al. (2009)
12 more