4ekd

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

Method: X-RAY DIFFRACTION Dmax: 76.0 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 CO COBALT (II) ION × 2 CL CHLORIDE ION × 2 MG MAGNESIUM ION × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;277 K;12% PEG 8,000, 15 mM CoCl2, 200 mM NaCl, and 100 mM MES 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.71 Å R-free 0.252

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 16 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

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 CO COBALT (II) ION × 2 CL CHLORIDE ION × 2 MG MAGNESIUM ION × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;277 K;12% PEG 8,000, 15 mM CoCl2, 200 mM NaCl, and 100 mM MES 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.71 Å R-free 0.252

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 4 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

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 4ekd

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4ekd
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 keywordsGTP-binding, Regulator of G protein signaling, 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_guinier23.77
Radius of gyration Rg (electron density) rg_electron22.80
Forward intensity I(0) i047481300.00
Molecular weight molecular_weight53390.0 kDa
Excluded volume excluded_volume66731 ų
Envelope volume envelope_volume80352 ų
Hydration-shell volume shell_volume28734 ų
Envelope diameter envelope_diameter79.0
Shell Rg shell_rg30.58
Envelope Rg envelope_rg23.11
Shape Rg shape_rg22.79
Total Rg total_rg23.74
Total atoms total_atoms3746
Residues n_residues450
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 dmax76.0
Rg (real space) rg_real23.63
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real4.7480e+07
I(0) uncertainty (real space) i0_real_error6.5530e+05
Rg (reciprocal space) rg_reciprocal23.66
I(0) (reciprocal space) i0_reciprocal47480000.0000
Solution quality estimate total_estimate0.8936
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary29.7
Skewness Skewness skewness0.189
Kurtosis Kurtosis kurtosis-0.398
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11700000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.876; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4ekdb1
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_idd4ekdb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (4 domains)

Domain ID domain_id4ekdA01
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_id4ekdA02
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_id4ekdB01
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_id4ekdB02
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)