SAXSdb — 3agw

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

G protein-activated inward rectifier potassium channel 2

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 53–74 Chain A； UniProt 200–381	Fragment：residues 53-74, 200-381	MG MAGNESIUM ION × 4 EOH ETHANOL × 8	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；7.5-12.5% EtOH, 0.1M Imidazole-HCl, 0.1M MgCl2, 0.003M spermine, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.20 Å R-free 0.236

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 3AGW	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3VSQ Crystal Structure of the Cytoplasmic Domain of G-Protein-Gated Inward Rectifier Potassium Channel Kir3.2 E236R Mutant in the presence of ethanol Deposited 2012-05-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 53–74（22 aa） Fragment：UNP residues 53-74, 200-381 Chain A 200–381（182 aa） Fragment：UNP residues 53-74, 200-381	Mutation：E236R Mutation：E236R	BME BETA-MERCAPTOETHANOL × 8 MG MAGNESIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；15%(v/v) ethanol, 0.1M HEPE-NaOH, 0.2M MgCl2, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.00 Å R-free 0.259
4KFM Crystal structure of the G protein-gated inward rectifier K+ channel GIRK2 (Kir3.2) in complex with the beta-gamma G protein subunits Deposited 2013-04-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 52–380（329 aa）	Not recorded	PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 4 K POTASSIUM ION × 20 NA SODIUM ION × 4 LMT DODECYL-BETA-D-MALTOSIDE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.8；293.15 K；600 mM NaK tartrate, 50 mM Na-ADA, pH 5.8, vapor diffusion, hanging drop, temperature 293.15K	Resolution 3.45 Å R-free 0.265

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q8C4T8_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–26； UniProt 53–74 Author chain A； PDBConstruct 27–208； UniProt 200–381

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	3agw
Deposition date deposition_date	2010-04-08
Structure title title	Crystal Structure of the Cytoplasmic Domain of G-Protein-Gated Inward Rectifier Potassium Channel Kir3.2 in the absence of Na+
Keywords keywords	cytoplasmic assembly, ion channel, beta-barrel, TRANSPORT PROTEIN; TRANSPORT 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	19.89 Å
Radius of gyration Rg (electron density) rg_electron	18.73 Å
Forward intensity I(0) i0	9236090.00
Molecular weight molecular_weight	22388.0 kDa
Excluded volume excluded_volume	28060 Å³
Envelope volume envelope_volume	35053 Å³
Hydration-shell volume shell_volume	16323 Å³
Envelope diameter envelope_diameter	68.8 Å
Shell Rg shell_rg	24.13 Å
Envelope Rg envelope_rg	19.16 Å
Shape Rg shape_rg	18.71 Å
Total Rg total_rg	19.69 Å
Total atoms total_atoms	1575
Residues n_residues	196
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	68.1 Å
Rg (real space) rg_real	19.91 Å
Rg uncertainty (real space) rg_real_error	0.44 Å
I(0) (real space) i0_real	9.2360e+06
I(0) uncertainty (real space) i0_real_error	1.2620e+05
Rg (reciprocal space) rg_reciprocal	19.91 Å
I(0) (reciprocal space) i0_reciprocal	9236000.0000
Solution quality estimate total_estimate	0.6902
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	23.0 Å
Skewness Skewness skewness	0.389
Kurtosis Kurtosis kurtosis	-0.177
Angular range angular_range	— – 0.4000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1349000.0000
Real-space data points n_real_points	72
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.798; Stabil: 1.000; Sysdev: 0.210; Positv: 1.000; Valcen: 0.948; Smooth: 0.998

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	G protein-activated inward rectifier potassium channel 2
Molecular weight formula_weight	23749.0 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1720

GSHMRKIQRYVRKDGKCNVHHGNVREKRAETLVFSTHAVISMRDGKLCLMFRVGDLRNSHIVEASIRAKLIKSKQTSEGEFIPLNQTDINVGYYTGDDRLFLVSPLIISHEINQQSPFWEISKAQLPKEELEIVVILEGMVEATGMTCQARSSYITSEILWGYRFTPVLTLEDGFYEVDYNSFHETYETSTPSLSAKELAELANRAEL

来源 Source

来源生物 organism	Mus musculus
通用名 common_name	mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	ETHANOL
Molecular weight formula_weight	46.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	140

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d3agwa_
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.18 — E set domains
Family Family family	b.1.18.16 — Cytoplasmic domain of inward rectifier potassium channel

CATH v4.4 (1 domains)

Domain ID domain_id	3agwA00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	1400 — G protein-activated inward rectifier potassium channel 1

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8. Citations (1)

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Unit-cell length a length_a	81.943 Å
Unit-cell length b length_b	81.943 Å
Unit-cell length c length_c	172.769 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	16

Space group space_group	I 4 2 2
Space-group number int_tables_number	97
Crystal system crystal_system	—

Resolution resolution	2.200 Å
Low-resolution limit resolution_low	29.730 Å
R factor r_factor	0.1998
R_work r_work	0.1979
R_free r_free	0.2358

fit	/app/data/saxs_computation/ag/3agw/3agw.fit
pddf	/app/data/pr_computation/ag/3agw/3agw.pr.out
profile	/app/data/saxs_computation/ag/3agw/3agw.dat

Crystal Structure of the Cytoplasmic Domain of G-Protein-Gated Inward Rectifier Potassium Channel Kir3.2 in the absence of Na+

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

G protein-activated inward rectifier potassium channel 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