SAXSdb — 9g9w

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

Potassium channel subfamily K member 9

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 1–265 Chain B； UniProt 1–265	Mutation：G236R	Y01 CHOLESTEROL HEMISUCCINATE × 6 K POTASSIUM ION × 3	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5；20 mM HEPES pH 7.5, 200 mM KCl, 0.12% w/v DM, 0.012% w/v CHS cryo-EM vitrification conditions：Cryogen ETHANE；Grid blotted for 4.5 seconds	Resolution 2.48 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 9G9W	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3P1N Crystal structure of human 14-3-3 sigma in complex with TASK-3 peptide Deposited 2010-09-30	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 P 369–374（6 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	MG MAGNESIUM ION × 6 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；277 K；0.095M HEPES Na-Salt, 25.6% PEG 400, 0.19M CaCl2, 5% Glycerol, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.40 Å R-free 0.174
3P1O Crystal structure of human 14-3-3 sigma in complex with TASK-3 peptide and stabilisator Fusicoccin A Deposited 2010-09-30	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 P 369–374（6 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	FSC FUSICOCCIN × 2 CL CHLORIDE ION × 2 CA CALCIUM ION × 2 MG MAGNESIUM ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；277 K；0.095M HEPES Na-Salt, 25.6% PEG 400, 0.19M CaCl2, 5% Glycerol, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.234
3P1P Crystal structure of human 14-3-3 sigma C38N/N166H in complex with TASK-3 peptide Deposited 2010-09-30	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 P 369–374（6 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	CL CHLORIDE ION × 2 MG MAGNESIUM ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；277.15 K；0.095M HEPES Na-Salt, 25.6% PEG 400, 0.19M CaCl2, 5% Glycerol, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 277.15K	Resolution 1.95 Å R-free 0.227
3P1Q Crystal structure of human 14-3-3 sigma C38N/N166H in complex with TASK-3 Peptide and stabilizer fusicoccin A Deposited 2010-09-30	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 P 369–374（6 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	FSC FUSICOCCIN × 2 CL CHLORIDE ION × 2 MG MAGNESIUM ION × 4 CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；277.15 K；0.095M HEPES Na-Salt, 25.6% PEG 400, 0.19M CaCl2, 5% Glycerol, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 277.15K	Resolution 1.70 Å R-free 0.217
3P1R Crystal structure of human 14-3-3 sigma C38V/N166H in complex with TASK-3 peptide Deposited 2010-09-30	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 P 369–374（6 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	MG MAGNESIUM ION × 8 CL CHLORIDE ION × 8 CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；277 K；0.095M HEPES Na-Salt, 25.6% PEG 400, 0.19M CaCl2, 5% Glycerol, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.70 Å R-free 0.194
3P1S Crystal structure of human 14-3-3 sigma C38N/N166H in complex with TASK-3 peptide and stabilizer fusicoccin A Deposited 2010-09-30	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 P 369–374（6 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	FSC FUSICOCCIN × 2 CL CHLORIDE ION × 2 MG MAGNESIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；277.15 K；0.095M HEPES Na-Salt, 25.6% PEG 400, 0.19M CaCl2, 5% Glycerol, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 277.15K	Resolution 1.65 Å R-free 0.201
3UX0 Crystal structure of human 14-3-3 sigma in complex with TASK-3 peptide and stabilizer Fusicoccin H Deposited 2011-12-03	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 P 369–374（6 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	MG MAGNESIUM ION × 8 CL CHLORIDE ION × 2 GOL GLYCEROL × 2 0DV (4R,5R,6R,6aS,9S,9aE,10aR)-5-hydroxy-9-(hydroxymethyl)-6,10a-dimethyl-3-(propan-2-yl)-1,2,4,5,6,6a,7,8,9,10a-decahydrod icyclopenta[a,d][8]annulen-4-yl alpha-D-gulopyranoside × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.095M HEPES Na, 0.19M calcium chloride, 5% glycerol, 26.6% PEG400, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.75 Å R-free 0.192
6GHP 14-3-3sigma in complex with a TASK3 peptide stabilized by semi-synthetic natural product FC-NAc Deposited 2018-05-08	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 P 368–374（7 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	EZ5 ~{N}-[(2~{S})-2-[(1~{E},3~{R},4~{S},8~{R},9~{R},10~{R},11~{S},14~{S})-14-(methoxymethyl)-3,10-dimethyl-8-[(2~{S},3~{R},4~{S},5~{S},6~{R})-6-(2-methylbut-3-en-2-yloxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-4,9-bis(oxidanyl)-6-tricyclo[9.3.0.0^{3,7}]tetradeca-1,6-dienyl]propyl]ethanamide × 2 CL CHLORIDE ION × 2 NA SODIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.1；278 K；0.095 M HEPES, pH 7.1, 26% v/v PEG400, 0.19 M CaCl2, 5% v/v glycerol	Resolution 1.95 Å R-free 0.231
8K1J Human TWIK-related acid-sensitive potassium channel TASK3 at pH 7.4,200 mM KCl Deposited 2023-07-11	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–259（259 aa） Chain B 1–259（259 aa）	Not recorded	Y01 CHOLESTEROL HEMISUCCINATE × 6 K POTASSIUM ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 3.00 Å
8K1Q Human TWIK-related acid-sensitive potassium channel TASK3 at pH 6.0, 5 mM KCl and 135 mM NaCl Deposited 2023-07-11	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–259（259 aa） Chain B 1–259（259 aa）	Not recorded	Y01 CHOLESTEROL HEMISUCCINATE × 6 K POTASSIUM ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 3.68 Å
8K1V Human TWIK-related acid-sensitive potassium channel TASK3 at pH 7.4, 5 mM KCl and 135 mM NaCl Deposited 2023-07-11	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–259（259 aa） Chain B 1–259（259 aa）	Not recorded	Y01 CHOLESTEROL HEMISUCCINATE × 6 K POTASSIUM ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 3.48 Å
8K1Z Human TWIK-related acid-sensitive potassium channel TASK3 at pH 6.0, 200 mM KCl Deposited 2023-07-11	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–259（259 aa） Chain B 1–259（259 aa）	Not recorded	Y01 CHOLESTEROL HEMISUCCINATE × 6 K POTASSIUM ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 6 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 3.41 Å
9G9V Structure of the human two pore domain potassium ion channel TASK-3 (K2P9.1) Deposited 2024-07-25	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–259（259 aa） Chain B 1–259（259 aa）	Not recorded	Y01 CHOLESTEROL HEMISUCCINATE × 4 K POTASSIUM ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；20 mM HEPES pH 7.5, 200 mM KCl, 0.12% w/v DM, 0.012% w/v CHS cryo-EM vitrification conditions Cryogen ETHANE；Grid blotted for 3 seconds	Resolution 3.32 Å

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	KCNK9_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–265； UniProt 1–265 Author chain B； PDBConstruct 1–265； UniProt 1–265

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	9g9w
Deposition date deposition_date	2024-07-25
Structure title title	Structure of the human two pore domain potassium ion channel TASK-3 (K2P9.1) G236R mutant
Keywords keywords	K2P, membrane protein, potassium channel, ion channel; 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	25.83 Å
Radius of gyration Rg (electron density) rg_electron	24.43 Å
Forward intensity I(0) i0	44152400.00
Molecular weight molecular_weight	58054.0 kDa
Excluded volume excluded_volume	75195 Å³
Envelope volume envelope_volume	89367 Å³
Hydration-shell volume shell_volume	30519 Å³
Envelope diameter envelope_diameter	89.1 Å
Shell Rg shell_rg	31.90 Å
Envelope Rg envelope_rg	24.81 Å
Shape Rg shape_rg	24.41 Å
Total Rg total_rg	25.40 Å
Total atoms total_atoms	4089
Residues n_residues	516
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	87.6 Å
Rg (real space) rg_real	25.82 Å
Rg uncertainty (real space) rg_real_error	0.60 Å
I(0) (real space) i0_real	4.4150e+07
I(0) uncertainty (real space) i0_real_error	6.4030e+05
Rg (reciprocal space) rg_reciprocal	25.82 Å
I(0) (reciprocal space) i0_reciprocal	44150000.0000
Solution quality estimate total_estimate	0.8529
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	86.1 Å
Skewness Skewness skewness	0.416
Kurtosis Kurtosis kurtosis	-0.022
Angular range angular_range	— – 0.3050 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	4918000.0000
Real-space data points n_real_points	62
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.719; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.928

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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	Potassium channel subfamily K member 9
Molecular weight formula_weight	30973.0 kDa
Mutation mutation	G236R
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	4089

MKRQNVRTLSLIVCTFTYLLVGAAVFDALESDHEMREEEKLKAEEIRIKGKYNISSEDYRQLELVILQSEPHRAGVQWKFAGSFYFAITVITTIGYGHAAPGTDAGKAFCMFYAVLGIPLTLVMFQSLGERMNTFVRYLLKRIKKCCGMRNTDVSMENMVTVGFFSCMGTLCIGAAAFSQCEEWSFFHAYYYCFITLTTIGFGDYVALQTKGALQKKPLYVAFSFMYILVGLTVIRAFLNLVVLRFLTMNSEDERRDAEERASLAAENLYFQ

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	Spodoptera frugiperda

Entity 2 Entity 2 non-polymer

Description description	CHOLESTEROL HEMISUCCINATE
Molecular weight formula_weight	486.7 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 3 Entity 3 non-polymer

Description description	POTASSIUM ION
Molecular weight formula_weight	39.1 kDa
Source method src_method	syn
Copy count entity_count	3

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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	2.48 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	124588

fit	/app/data/saxs_computation/g9/9g9w/9g9w.fit
pddf	/app/data/pr_computation/g9/9g9w/9g9w.pr.out
profile	/app/data/saxs_computation/g9/9g9w/9g9w.dat

Structure of the human two pore domain potassium ion channel TASK-3 (K2P9.1) G236R mutant

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

Potassium channel subfamily K member 9

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