7v9l

Cryo-EM structure of the SV1-Gs complex.

Method: ELECTRON MICROSCOPY Dmax: 114.3 Å Quality: GOOD

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

GHRH receptor splice variant 1,GHRH receptor splice variant 1,GHRH receptor splice variant 1,SV1

Homo sapiens

UniProt Q9HB45

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain R; UniProt 1–341 Not recorded Guanine nucleotide-binding protein G(s) subunit alpha isoforms short × 1 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P63212) Nanobody 35 × 1 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P54311) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q9HB45_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain R; PDBConstruct 1–341; UniProt 1–341

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2

Bos taurus

UniProt P63212

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain Y; UniProt 1–71 Not recorded Guanine nucleotide-binding protein G(s) subunit alpha isoforms short × 1 GHRH receptor splice variant 1,GHRH receptor splice variant 1,GHRH receptor splice variant 1,SV1 × 1 (Q9HB45) Nanobody 35 × 1 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P54311) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

215 other PDB entries and 216 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBG2_BOVIN
Isoform
PDB entities 3
Chains and sequence ranges Author chain Y; PDBConstruct 1–71; UniProt 1–71

Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1

Rattus norvegicus

UniProt P54311

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 2–340 Not recorded Guanine nucleotide-binding protein G(s) subunit alpha isoforms short × 1 GHRH receptor splice variant 1,GHRH receptor splice variant 1,GHRH receptor splice variant 1,SV1 × 1 (Q9HB45) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P63212) Nanobody 35 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

161 other PDB entries and 162 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBB1_RAT
Isoform
PDB entities 5
Chains and sequence ranges Author chain B; PDBConstruct 7–345; UniProt 2–340

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 7v9l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7v9l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7v9l
Deposition date deposition_date2021-08-26
Structure title titleCryo-EM structure of the SV1-Gs complex.
Keywords keywordsclass B GPCR, receptor bias, cancer, cell proliferation, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier33.17
Radius of gyration Rg (electron density) rg_electron33.14
Forward intensity I(0) i0203171000.00
Molecular weight molecular_weight114320.0 kDa
Excluded volume excluded_volume143100 ų
Envelope volume envelope_volume177460 ų
Hydration-shell volume shell_volume45014 ų
Envelope diameter envelope_diameter120.3
Shell Rg shell_rg39.34
Envelope Rg envelope_rg33.43
Shape Rg shape_rg33.15
Total Rg total_rg33.59
Total atoms total_atoms8047
Residues n_residues1019
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 dmax114.3
Rg (real space) rg_real33.27
Rg uncertainty (real space) rg_real_error0.95
I(0) (real space) i0_real2.0320e+08
I(0) uncertainty (real space) i0_real_error3.0160e+06
Rg (reciprocal space) rg_reciprocal33.23
I(0) (reciprocal space) i0_reciprocal203200000.0000
Solution quality estimate total_estimate0.8596
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.1
Skewness Skewness skewness0.465
Kurtosis Kurtosis kurtosis-0.122
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha47110000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.792; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.960; Smooth: 0.836

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7v9lB01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id7v9lN01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)