SAXSdb — 2a72

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

Regulator of G-protein signalling 7

Homo sapiens

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 320–463 Chain B； UniProt 320–463	Fragment：RESIDUES 320-463	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；PEG 3350, (NH4)2SO4, BIS-TRIS, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.00 Å R-free 0.249

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 2A72	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2D9J Solution structure of the RGS domain of Regulator of G-protein signaling 7 Deposited 2005-12-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 323–448（126 aa） Fragment：RGS domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient NMR sample composition 1.33mM 13C, 15N-labeled protein; 20mM d-Tris-HCl(pH7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3 \| 90% H2O/10% D2O	Resolution not provided
7EWP Cryo-EM structure of human GPR158 in complex with RGS7-Gbeta5 in a 2:1:1 ratio Deposited 2021-05-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–495（495 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.30 Å
7EWR Cryo-EM structure of human GPR158 in complex with RGS7-Gbeta5 in a 2:2:2 ratio Deposited 2021-05-26	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain C 1–495（495 aa） Chain E 1–495（495 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.70 Å
7SHF Cryo-EM structure of GPR158 coupled to the RGS7-Gbeta5 complex Deposited 2021-10-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–469（469 aa）	Not recorded	CLR CHOLESTEROL × 22 EIJ (2S)-1-{[(S)-hydroxy{[(1s,2R,3R,4R,5S,6S)-2,3,4,5,6-pentahydroxycyclohexyl]oxy}phosphoryl]oxy}-3-(octadecanoyloxy)propan-2-yl (5E,8E,11E,14E)-icosa-5,8,11,14-tetraenoate × 1 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å

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 A； PDBConstruct 3–146； UniProt 320–463 Author chain B； PDBConstruct 3–146； UniProt 320–463

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	2a72
Deposition date deposition_date	2005-07-04
Structure title title	Structure of the regulator of G-protein signaling domain of RGS7
Keywords keywords	;Human RGS7, regulator of G-protein signaling 7, GTPase-activating proteins (GAP), Structural Genomics, Structural Genomics Consortium, SGC, SIGNALING PROTEIN ;; SIGNALING PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	25.61 Å
Radius of gyration Rg (electron density) rg_electron	25.26 Å
Forward intensity I(0) i0	16102800.00
Molecular weight molecular_weight	30664.0 kDa
Excluded volume excluded_volume	38394 Å³
Envelope volume envelope_volume	48690 Å³
Hydration-shell volume shell_volume	17971 Å³
Envelope diameter envelope_diameter	93.2 Å
Shell Rg shell_rg	29.56 Å
Envelope Rg envelope_rg	25.80 Å
Shape Rg shape_rg	25.23 Å
Total Rg total_rg	25.92 Å
Total atoms total_atoms	2168
Residues n_residues	266
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	91.3 Å
Rg (real space) rg_real	25.93 Å
Rg uncertainty (real space) rg_real_error	0.97 Å
I(0) (real space) i0_real	1.6100e+07
I(0) uncertainty (real space) i0_real_error	2.5180e+05
Rg (reciprocal space) rg_reciprocal	25.83 Å
I(0) (reciprocal space) i0_reciprocal	16100000.0000
Solution quality estimate total_estimate	0.7893
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	20.6 Å
Skewness Skewness skewness	0.604
Kurtosis Kurtosis kurtosis	-0.202
Angular range angular_range	— – 0.3100 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3751000.0000
Real-space data points n_real_points	63
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.618; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.491; Smooth: 0.911

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Regulator of G-protein signalling 7
Molecular weight formula_weight	17138.4 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	2413

SMKEPSQQRVKRWGFGMDEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKKRPIKEVPSRVQEIWQEFLAPGAPSAINLDSKSYDKTTHNVKEPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQELLQAKKKSGNSMDRRTS

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	231

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7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d2a72a1
Class class	a — All alpha proteins
Fold Fold fold	a.91 — Regulator of G-protein signaling, RGS
Superfamily Superfamily superfamily	a.91.1 — Regulator of G-protein signaling, RGS
Family Family family	a.91.1.0 — automated matches

Domain ID domain_id	d2a72a2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d2a72b1
Class class	a — All alpha proteins
Fold Fold fold	a.91 — Regulator of G-protein signaling, RGS
Superfamily Superfamily superfamily	a.91.1 — Regulator of G-protein signaling, RGS
Family Family family	a.91.1.0 — automated matches

Domain ID domain_id	d2a72b2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id	2a72A00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	167 — Regulator of G-protein Signalling 4; domain 2
Homologous superfamily homologous superfamily	10 — Regulator of G-protein Signalling 4, domain 2

Domain ID domain_id	2a72B00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	167 — Regulator of G-protein Signalling 4; domain 2
Homologous superfamily homologous superfamily	10 — Regulator of G-protein Signalling 4, domain 2

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8. Citations (1)

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Unit-cell length a length_a	28.915 Å
Unit-cell length b length_b	106.033 Å
Unit-cell length c length_c	52.490 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	103.71 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	53.000 Å
R factor r_factor	0.1876
R_work r_work	0.1842
R_free r_free	0.2489

fit	/app/data/saxs_computation/a7/2a72/2a72.fit
pddf	/app/data/pr_computation/a7/2a72/2a72.pr.out
profile	/app/data/saxs_computation/a7/2a72/2a72.dat

Structure of the regulator of G-protein signaling domain of RGS7

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

Regulator of G-protein signalling 7

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

Refinement Refinement

Diffraction experiment Diffraction