2ode

Crystal structure of the heterodimeric complex of human RGS8 and activated Gi alpha 3

Method: X-RAY DIFFRACTION Dmax: 97.8 Å Quality: EXCELLENT

1. Protein Identity and Related Structures Protein Identity & Related Structures

Guanine nucleotide-binding protein G(k) subunit alpha

Homo sapiens

UniProt P08754

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 4–350 Not recorded Regulator of G-protein signaling 8 × 1 (P57771) ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.20M NH4Cl, 20.0% PEG 6K, 10.0% EtGly, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.90 Å R-free 0.211
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 4–350 Not recorded Regulator of G-protein signaling 8 × 1 (P57771) ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.20M NH4Cl, 20.0% PEG 6K, 10.0% EtGly, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.90 Å R-free 0.211

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

24 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GNAI3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–349; UniProt 4–350 Author chain C; PDBConstruct 3–349; UniProt 4–350

Regulator of G-protein signaling 8

Homo sapiens

UniProt P57771

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 42–180 Fragment:residues 42-180 Guanine nucleotide-binding protein G(k) subunit alpha × 1 (P08754) ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.20M NH4Cl, 20.0% PEG 6K, 10.0% EtGly, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.90 Å R-free 0.211
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 42–180 Fragment:residues 42-180 Guanine nucleotide-binding protein G(k) subunit alpha × 1 (P08754) ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.20M NH4Cl, 20.0% PEG 6K, 10.0% EtGly, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.90 Å R-free 0.211

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

2 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RGS8_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–141; UniProt 42–180 Author chain D; PDBConstruct 3–141; UniProt 42–180

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 2ode

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2ode
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2ode
Deposition date deposition_date2006-12-22
Structure title titleCrystal structure of the heterodimeric complex of human RGS8 and activated Gi alpha 3
Keywords keywords;G protein signalling, RGS, heterotrimeric G protein, signalling complex, Structural Genomics, Structural Genomics Consortium, SGC, SIGNALING PROTEIN ;; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier31.05
Radius of gyration Rg (electron density) rg_electron30.37
Forward intensity I(0) i0160894000.00
Molecular weight molecular_weight100240.0 kDa
Excluded volume excluded_volume125020 ų
Envelope volume envelope_volume155920 ų
Hydration-shell volume shell_volume41831 ų
Envelope diameter envelope_diameter98.6
Shell Rg shell_rg38.33
Envelope Rg envelope_rg30.22
Shape Rg shape_rg30.39
Total Rg total_rg30.98
Total atoms total_atoms7048
Residues n_residues880
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax97.8
Rg (real space) rg_real30.95
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real1.6090e+08
I(0) uncertainty (real space) i0_real_error2.4250e+06
Rg (reciprocal space) rg_reciprocal31.00
I(0) (reciprocal space) i0_reciprocal160900000.0000
Solution quality estimate total_estimate0.9051
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary36.4
Skewness Skewness skewness0.238
Kurtosis Kurtosis kurtosis-0.528
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha30090000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.935; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.957

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2odeb_
Class classa — All alpha proteins
Fold Fold folda.91 — Regulator of G-protein signaling, RGS
Superfamily Superfamily superfamilya.91.1 — Regulator of G-protein signaling, RGS
Family Family familya.91.1.1 — Regulator of G-protein signaling, RGS
Domain ID domain_idd2oded_
Class classa — All alpha proteins
Fold Fold folda.91 — Regulator of G-protein signaling, RGS
Superfamily Superfamily superfamilya.91.1 — Regulator of G-protein signaling, RGS
Family Family familya.91.1.1 — Regulator of G-protein signaling, RGS

CATH v4.4 (8 domains)

Domain ID domain_id2odeA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id2odeA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology400 — GI Alpha 1, domain 2-like
Homologous superfamily homologous superfamily10 — GI Alpha 1, domain 2-like
Domain ID domain_id2odeB01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology196 — Regulator of G-protein Signalling 4; domain 1
Homologous superfamily homologous superfamily10
Domain ID domain_id2odeB02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology167 — Regulator of G-protein Signalling 4; domain 2
Homologous superfamily homologous superfamily10 — Regulator of G-protein Signalling 4, domain 2
Domain ID domain_id2odeC01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id2odeC02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology400 — GI Alpha 1, domain 2-like
Homologous superfamily homologous superfamily10 — GI Alpha 1, domain 2-like
Domain ID domain_id2odeD01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology196 — Regulator of G-protein Signalling 4; domain 1
Homologous superfamily homologous superfamily10
Domain ID domain_id2odeD02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology167 — Regulator of G-protein Signalling 4; domain 2
Homologous superfamily homologous superfamily10 — Regulator of G-protein Signalling 4, domain 2

8. Citations (1)

9. Files and Curves (10)