SAXSdb — 2af0

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

Regulator of G-protein signaling 2

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 71–203	Fragment：residues 71-203	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.5；298 K；(NH4)2SO4, NaCl, cacodylate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 2.30 Å R-free 0.256

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 2AF0	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2V4Z The crystal structure of the human G-protein subunit alpha (GNAI3) in complex with an engineered regulator of G-protein signaling type 2 domain (RGS2) Deposited 2008-09-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 71–209（139 aa） Fragment：RGS DOMAIN, RESIDUES 71-209	Mutation：YES	GDP GUANOSINE-5'-DIPHOSPHATE × 1 ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；0.1 M HEPES PH 7.5, 2 M AMMONIUM SULPHATE	Resolution 2.80 Å R-free 0.254
4EKC Structure of human regulator of G protein signaling 2 (RGS2) in complex with murine Galpha-q(R183C) Deposited 2012-04-09	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 72–203（132 aa） Fragment：RGS domain, UNP residues 72-203	Not recorded	GDP GUANOSINE-5'-DIPHOSPHATE × 1 ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；17% PEG 3350, 200 mM NaCl, and 100 mM MES pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 7.40 Å R-free 0.220
4EKC Structure of human regulator of G protein signaling 2 (RGS2) in complex with murine Galpha-q(R183C) Deposited 2012-04-09	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 72–203（132 aa） Fragment：RGS domain, UNP residues 72-203	Not recorded	GDP GUANOSINE-5'-DIPHOSPHATE × 1 ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；17% PEG 3350, 200 mM NaCl, and 100 mM MES pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 7.40 Å R-free 0.220
4EKD Structure of human regulator of G protein signaling 2 (RGS2) in complex with murine Galpha-q(R183C) Deposited 2012-04-09	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 72–203（132 aa） Fragment：RGS domain, UNP residues 72-203	Not recorded	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

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	1
Chains and sequence ranges	Author chain A； PDBConstruct 14–146； UniProt 71–203

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2af0
Deposition date deposition_date	2005-07-25
Structure title title	Structure of the Regulator of G-Protein Signaling Domain of RGS2
Keywords keywords	HELIX, 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	18.65 Å
Radius of gyration Rg (electron density) rg_electron	17.69 Å
Forward intensity I(0) i0	4975840.00
Molecular weight molecular_weight	16183.0 kDa
Excluded volume excluded_volume	20256 Å³
Envelope volume envelope_volume	24417 Å³
Hydration-shell volume shell_volume	12536 Å³
Envelope diameter envelope_diameter	65.2 Å
Shell Rg shell_rg	22.63 Å
Envelope Rg envelope_rg	18.31 Å
Shape Rg shape_rg	17.68 Å
Total Rg total_rg	18.67 Å
Total atoms total_atoms	1144
Residues n_residues	146
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	66.3 Å
Rg (real space) rg_real	18.76 Å
Rg uncertainty (real space) rg_real_error	0.55 Å
I(0) (real space) i0_real	4.9760e+06
I(0) uncertainty (real space) i0_real_error	6.4210e+04
Rg (reciprocal space) rg_reciprocal	18.75 Å
I(0) (reciprocal space) i0_reciprocal	4976000.0000
Solution quality estimate total_estimate	0.8309
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	18.2 Å
Skewness Skewness skewness	0.490
Kurtosis Kurtosis kurtosis	-0.205
Angular range angular_range	— – 0.4250 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	866300.0000
Real-space data points n_real_points	74
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.685; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.779; Smooth: 0.962

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2af0a1
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	d2af0a2
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	2af0A01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	196 — Regulator of G-protein Signalling 4; domain 1
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	2af0A02
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	43.754 Å
Unit-cell length b length_b	43.754 Å
Unit-cell length c length_c	158.451 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	8

Space group space_group	P 43 21 2
Space-group number int_tables_number	96
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	33.690 Å
R factor r_factor	0.2272
R_work r_work	0.2258
R_free r_free	0.2561

Description description	Regulator of G-protein signaling 2
Molecular weight formula_weight	16994.1 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1166

Structure of the Regulator of G-Protein Signaling Domain of RGS2

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

Regulator of G-protein signaling 2

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

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

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

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	17

fit	/app/data/saxs_computation/af/2af0/2af0.fit
pddf	/app/data/pr_computation/af/2af0/2af0.pr.out
profile	/app/data/saxs_computation/af/2af0/2af0.dat