4ekc

Structure of human regulator of G protein signaling 2 (RGS2) in complex with murine Galpha-q(R183C)

Method: X-RAY DIFFRACTION Dmax: 121.2 Å Quality: GOOD

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

Guanine nucleotide-binding protein G(q) subunit alpha

Mus musculus

UniProt P21279

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 18–359 Fragment:UNP residues 18-359 Mutation:E125D, N126V, Y128D, V129Y, D130A, R183C Regulator of G-protein signaling 2 × 1 (P41220) GDP GUANOSINE-5'-DIPHOSPHATE × 1 ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;277 K;17% PEG 3350, 200 mM NaCl, and 100 mM MES pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 7.40 Å R-free 0.220
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 18–359 Fragment:UNP residues 18-359 Mutation:E125D, N126V, Y128D, V129Y, D130A, R183C Regulator of G-protein signaling 2 × 1 (P41220) GDP GUANOSINE-5'-DIPHOSPHATE × 1 ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;277 K;17% PEG 3350, 200 mM NaCl, and 100 mM MES pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 7.40 Å R-free 0.220

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.

9 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GNAQ_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–347; UniProt 18–359 Author chain C; PDBConstruct 6–347; UniProt 18–359

Regulator of G-protein signaling 2

Homo sapiens

UniProt P41220

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 72–203 Fragment:RGS domain, UNP residues 72-203 Guanine nucleotide-binding protein G(q) subunit alpha × 1 (P21279) GDP GUANOSINE-5'-DIPHOSPHATE × 1 ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;277 K;17% PEG 3350, 200 mM NaCl, and 100 mM MES pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 7.40 Å R-free 0.220
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 72–203 Fragment:RGS domain, UNP residues 72-203 Guanine nucleotide-binding protein G(q) subunit alpha × 1 (P21279) GDP GUANOSINE-5'-DIPHOSPHATE × 1 ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;277 K;17% PEG 3350, 200 mM NaCl, and 100 mM MES pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 7.40 Å R-free 0.220

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RGS2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 6–137; UniProt 72–203 Author chain D; PDBConstruct 6–137; UniProt 72–203

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 4ekc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4ekc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4ekc
Deposition date deposition_date2012-04-09
Structure title titleStructure of human regulator of G protein signaling 2 (RGS2) in complex with murine Galpha-q(R183C)
Keywords keywords;GTP-binding protein fold, Regulator, G protein signaling, RGS, homology domain, GTPase activation, SIGNALING PROTEIN-INHIBITOR complex ;; SIGNALING PROTEIN/INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.58
Radius of gyration Rg (electron density) rg_electron37.82
Forward intensity I(0) i0166879000.00
Molecular weight molecular_weight104980.0 kDa
Excluded volume excluded_volume131450 ų
Envelope volume envelope_volume179860 ų
Hydration-shell volume shell_volume40799 ų
Envelope diameter envelope_diameter129.9
Shell Rg shell_rg42.41
Envelope Rg envelope_rg37.48
Shape Rg shape_rg37.83
Total Rg total_rg38.09
Total atoms total_atoms7386
Residues n_residues890
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 dmax121.2
Rg (real space) rg_real37.82
Rg uncertainty (real space) rg_real_error0.89
I(0) (real space) i0_real1.6690e+08
I(0) uncertainty (real space) i0_real_error2.9300e+06
Rg (reciprocal space) rg_reciprocal37.68
I(0) (reciprocal space) i0_reciprocal166900000.0000
Solution quality estimate total_estimate0.8341
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.8
Skewness Skewness skewness0.375
Kurtosis Kurtosis kurtosis-0.741
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha41210000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.747; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.875; Smooth: 0.723

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)