SAXSdb — 9jvh

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

G-protein coupled receptor 4

Mus musculus

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain R； UniProt 1–365	Not recorded	No other associated polymer	ELECTRON MICROSCOPY cryo-EM buffer：pH 6.2 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.76 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.

Other PDB	Difference from Current Entry 9JVH	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
8ZF9 Cryo-EM structure of the mmGPR4-Gs complex in pH7.2 Deposited 2024-05-07	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain R 1–365（365 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.56 Å
8ZFC Cryo-EM structure of the mmGPR4-Gs complex in pH7.6 Deposited 2024-05-07	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain R 1–365（365 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.68 Å
8ZFD Cryo-EM structure of the mmGPR4-Gs receptor in pH7.6 Deposited 2024-05-07	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain R 1–365（365 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.56 Å
8ZFE Cryo-EM structure of the mmGPR4-Gs receptor in pH7.2 Deposited 2024-05-07	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain R 1–365（365 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.56 Å
9JVG Cryo-EM structure of the mmGPR4-Gs complex in pH6.2 Deposited 2024-10-09	Different oligomeric state	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain R 1–365（365 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.76 Å

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

View Construct and Data Evidence

UniProt name	GPR4_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain R； PDBConstruct 1–365； UniProt 1–365

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	9jvh
Deposition date deposition_date	2024-10-09
Structure title title	Cryo-EM structure of the mmGPR4-Gs receptor in pH6.2
Keywords keywords	pH6.2, mmGPR4, Gs, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	21.47 Å
Radius of gyration Rg (electron density) rg_electron	20.31 Å
Forward intensity I(0) i0	14990000.00
Molecular weight molecular_weight	30808.0 kDa
Excluded volume excluded_volume	39236 Å³
Envelope volume envelope_volume	46646 Å³
Hydration-shell volume shell_volume	19644 Å³
Envelope diameter envelope_diameter	74.5 Å
Shell Rg shell_rg	26.41 Å
Envelope Rg envelope_rg	20.79 Å
Shape Rg shape_rg	20.33 Å
Total Rg total_rg	21.19 Å
Total atoms total_atoms	2180
Residues n_residues	294
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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

Maximum dimension Dmax dmax	70.9 Å
Rg (real space) rg_real	21.51 Å
Rg uncertainty (real space) rg_real_error	0.56 Å
I(0) (real space) i0_real	1.4990e+07
I(0) uncertainty (real space) i0_real_error	2.1930e+05
Rg (reciprocal space) rg_reciprocal	21.50 Å
I(0) (reciprocal space) i0_reciprocal	14990000.0000
Solution quality estimate total_estimate	0.8002
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	24.0 Å
Skewness Skewness skewness	0.404
Kurtosis Kurtosis kurtosis	-0.362
Angular range angular_range	— – 0.3700 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2681000.0000
Real-space data points n_real_points	69
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.813; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.961; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	2.76 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	193910

Description description	G-protein coupled receptor 4
Molecular weight formula_weight	41149.8 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	R
Atom count atom_count	2180

Cryo-EM structure of the mmGPR4-Gs receptor in pH6.2

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

G-protein coupled receptor 4

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

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

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Mus musculus
通用名 common_name	house mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Spodoptera frugiperda

fit	/app/data/saxs_computation/jv/9jvh/9jvh.fit
pddf	/app/data/pr_computation/jv/9jvh/9jvh.pr.out
profile	/app/data/saxs_computation/jv/9jvh/9jvh.dat