7ewr

Cryo-EM structure of human GPR158 in complex with RGS7-Gbeta5 in a 2:2:2 ratio

Method: ELECTRON MICROSCOPY Dmax: 206.1 Å Quality: REASONABLE

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

Regulator of G-protein signaling 7

Homo sapiens

UniProt P49802

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 1–495 Chain E; UniProt 1–495 Not recorded Guanine nucleotide-binding protein subunit beta-5 × 2 (O14775) Probable G-protein coupled receptor 158 × 2 (Q5T848) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.70 Å

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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RGS7_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 1–495; UniProt 1–495 Author chain E; PDBConstruct 1–495; UniProt 1–495

Guanine nucleotide-binding protein subunit beta-5

Homo sapiens

UniProt O14775

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain D; UniProt 1–395 Chain F; UniProt 1–395 Not recorded Regulator of G-protein signaling 7 × 2 (P49802) Probable G-protein coupled receptor 158 × 2 (Q5T848) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.70 Å

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.

31 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GNB5_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–395; UniProt 1–395 Author chain F; PDBConstruct 1–395; UniProt 1–395

Probable G-protein coupled receptor 158

Homo sapiens

UniProt Q5T848

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–863 Chain B; UniProt 1–863 Not recorded Regulator of G-protein signaling 7 × 2 (P49802) Guanine nucleotide-binding protein subunit beta-5 × 2 (O14775) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.70 Å

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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GP158_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–863; UniProt 1–863 Author chain B; PDBConstruct 1–863; UniProt 1–863

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 7ewr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7ewr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7ewr
Deposition date deposition_date2021-05-26
Structure title titleCryo-EM structure of human GPR158 in complex with RGS7-Gbeta5 in a 2:2:2 ratio
Keywords keywordsGPCR, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier70.12
Radius of gyration Rg (electron density) rg_electron69.17
Forward intensity I(0) i01044550000.00
Molecular weight molecular_weight269350.0 kDa
Excluded volume excluded_volume336020 ų
Envelope volume envelope_volume613070 ų
Hydration-shell volume shell_volume80041 ų
Envelope diameter envelope_diameter229.5
Shell Rg shell_rg59.69
Envelope Rg envelope_rg69.21
Shape Rg shape_rg69.34
Total Rg total_rg68.33
Total atoms total_atoms25779
Residues n_residues2516
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 dmax206.1
Rg (real space) rg_real70.34
Rg uncertainty (real space) rg_real_error1.40
I(0) (real space) i0_real1.0440e+09
I(0) uncertainty (real space) i0_real_error2.2620e+07
Rg (reciprocal space) rg_reciprocal68.76
I(0) (reciprocal space) i0_reciprocal1041000000.0000
Solution quality estimate total_estimate0.6000
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary84.3
Skewness Skewness skewness0.350
Kurtosis Kurtosis kurtosis-0.702
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0023
Highest regularization parameter α highest_alpha30110000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.965; Stabil: 0.999; Sysdev: 0.006; Positv: 1.000; Valcen: 0.886; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)