SAXSdb — 6syg

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

Potassium voltage-gated channel subfamily H member 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 734–864	Not recorded	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；292 K；20% w/v PEG 3350, 2% v/v Tacsimate, 0.1M Bis-Tris, pH 6.8	Resolution 1.50 Å R-free 0.184

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 6SYG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BYW STRUCTURE OF THE N-TERMINAL DOMAIN OF THE HUMAN-ERG POTASSIUM CHANNEL Deposited 1998-10-15	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 26–135（110 aa） Fragment：N-TERMINAL DOMAIN	Mutation：R73C	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；PROTEIN SOLUTION AT 10MG/ML IN 10MM DTT, 5 MM N-OCTYL-GLUCO MIXED WITH EQUAL VOLUME OF 100 MM HEPES PH 7.0, 0.8-1.0 M SODIUM AND POTASSIUM TARTRAT	Resolution 2.60 Å R-free 0.286
1UJL Solution Structure of the HERG K+ channel S5-P extracellular linker Deposited 2003-08-05	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 570–611（42 aa） Fragment：RESIDUES 1-42	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.3；303 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR sample composition 1.4mM S5-P peptide \| 100mM SDS, 90% H2O, 10% D2O	Resolution not provided
2L1M Solution structure of the eag domain of the hERG (Kv11.1) K+ channel Deposited 2010-07-29	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–135（135 aa） Fragment：UNP residues 1-135	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5；298 K；Ionic strength (raw mmCIF value) 0.02；Pressure ambient NMR sample composition 0.4 mM [U-100% 13C; U-100% 15N] protein, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.4 mM [U-100% 15N] protein, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2L4R NMR solution structure of the N-terminal PAS domain of hERG Deposited 2010-10-13	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–135（135 aa） Fragment：UNP RESIDUES 1-135	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 150；Pressure AMBIENT NMR sample composition 0.5-1 mM [U-99% 13C; U-99% 15N] entity-1, 5 mM DTT-2, 1 mM EDTA-3, 150 mM sodium chloride-4, 20 mM sodium phosphate-5, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2LE7 Solution nmr structure of the S4S5 linker of herg potassium channel Deposited 2011-06-13	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 532–551（20 aa） Fragment：residues 532-551	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.6；300 K；Pressure AMBIENT NMR sample composition 100mM DPC-1, 90%(v/v) H2O-2, 10%(v/v) [U-2H] D2O-3, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2N7G Structure of the cyclic nucleotide-binding homology domain of the hERG channel Deposited 2015-09-10	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 734–864（131 aa） Fragment：UNP residues 734-869	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.2；298 K；Ionic strength (raw mmCIF value) 170；Pressure ambient NMR sample composition 0.4 mM [U-100% 13C; U-100% 15N] the cyclic nucleotide-binding homology domain of the hERG channel-1, 20 mM sodium phosphate-2, 150 mM sodium chloride-3, 1 mM DTT-4, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
4HP9 Crystal structure of the N-terminal truncated PAS domain from the hERG potassium channel Deposited 2012-10-23	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 10–135（126 aa） Fragment：PAS domain of KCNH channel, UNP residues 10-135	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；30% PEG-MME2000, 0.1M potasiumm thiocyanate, 1.0% benzamidine-HCl, vapor diffusion, sitting drop, temperature 298K	Resolution 2.12 Å R-free 0.238
4HQA Crystal structure of PAS domain from the human ERG (hERG) potassium channel Deposited 2012-10-25	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–135（135 aa） Fragment：PAS domain of KCNH channel, UNP residues 1-135	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；298 K；1.0M sodium/potassium tartrate, 0.1M Hepes, pH 7.0, vapor diffusion, sitting drop, temperature 298K	Resolution 1.96 Å R-free 0.239
5VA1 Cryo-EM structure of the human ether-a-go-go related K+ channel Deposited 2017-03-24	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–140（140 aa） Fragment：UNP residues 1-140,381-870,1006-1159 Chain A 381–870（490 aa） Fragment：UNP residues 1-140,381-870,1006-1159 Chain A 1006–1159（154 aa） Fragment：UNP residues 1-140,381-870,1006-1159	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；pH 7.4, adjusted with NaOH cryo-EM vitrification conditions Cryogen ETHANE；one blot: 3 second blot time, 0 blot force	Resolution 3.70 Å
5VA1 Cryo-EM structure of the human ether-a-go-go related K+ channel Deposited 2017-03-24	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–140（140 aa） Fragment：UNP residues 1-140,381-870,1006-1159 Chain A 381–870（490 aa） Fragment：UNP residues 1-140,381-870,1006-1159 Chain A 1006–1159（154 aa） Fragment：UNP residues 1-140,381-870,1006-1159	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；pH 7.4, adjusted with NaOH cryo-EM vitrification conditions Cryogen ETHANE；one blot: 3 second blot time, 0 blot force	Resolution 3.70 Å
5VA1 Cryo-EM structure of the human ether-a-go-go related K+ channel Deposited 2017-03-24	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–140（140 aa） Fragment：UNP residues 1-140,381-870,1006-1159 Chain A 381–870（490 aa） Fragment：UNP residues 1-140,381-870,1006-1159 Chain A 1006–1159（154 aa） Fragment：UNP residues 1-140,381-870,1006-1159	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；pH 7.4, adjusted with NaOH cryo-EM vitrification conditions Cryogen ETHANE；one blot: 3 second blot time, 0 blot force	Resolution 3.70 Å
5VA2 Cryo-EM structure of the human ether-a-go-go related K+ channel Deposited 2017-03-24	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–140（140 aa） Fragment：UNP residues 1-140,381-870,1006-1159 Chain A 351–870（520 aa） Fragment：UNP residues 1-140,381-870,1006-1159 Chain A 1006–1159（154 aa） Fragment：UNP residues 1-140,381-870,1006-1159	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；pH 7.4, adjusted with NaOH cryo-EM vitrification conditions Cryogen ETHANE；one blot: 3 second blot time, 0 blot force	Resolution 3.80 Å
5VA2 Cryo-EM structure of the human ether-a-go-go related K+ channel Deposited 2017-03-24	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–140（140 aa） Fragment：UNP residues 1-140,381-870,1006-1159 Chain A 351–870（520 aa） Fragment：UNP residues 1-140,381-870,1006-1159 Chain A 1006–1159（154 aa） Fragment：UNP residues 1-140,381-870,1006-1159	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；pH 7.4, adjusted with NaOH cryo-EM vitrification conditions Cryogen ETHANE；one blot: 3 second blot time, 0 blot force	Resolution 3.80 Å
5VA2 Cryo-EM structure of the human ether-a-go-go related K+ channel Deposited 2017-03-24	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–140（140 aa） Fragment：UNP residues 1-140,381-870,1006-1159 Chain A 351–870（520 aa） Fragment：UNP residues 1-140,381-870,1006-1159 Chain A 1006–1159（154 aa） Fragment：UNP residues 1-140,381-870,1006-1159	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；pH 7.4, adjusted with NaOH cryo-EM vitrification conditions Cryogen ETHANE；one blot: 3 second blot time, 0 blot force	Resolution 3.80 Å
5VA3 Cryo-EM structure of the human ether-a-go-go related K+ channel Deposited 2017-03-24	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–140（140 aa） Fragment：UNP residues 1-140,381-870,1006-1159 Chain A 381–870（490 aa） Fragment：UNP residues 1-140,381-870,1006-1159 Chain A 1006–1159（154 aa） Fragment：UNP residues 1-140,381-870,1006-1159	Mutation：S631A Mutation：S631A Mutation：S631A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；pH 7.4, adjusted with NaOH cryo-EM vitrification conditions Cryogen ETHANE；one blot: 3 second blot time, 0 blot force	Resolution 4.00 Å
5VA3 Cryo-EM structure of the human ether-a-go-go related K+ channel Deposited 2017-03-24	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–140（140 aa） Fragment：UNP residues 1-140,381-870,1006-1159 Chain A 381–870（490 aa） Fragment：UNP residues 1-140,381-870,1006-1159 Chain A 1006–1159（154 aa） Fragment：UNP residues 1-140,381-870,1006-1159	Mutation：S631A Mutation：S631A Mutation：S631A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；pH 7.4, adjusted with NaOH cryo-EM vitrification conditions Cryogen ETHANE；one blot: 3 second blot time, 0 blot force	Resolution 4.00 Å
5VA3 Cryo-EM structure of the human ether-a-go-go related K+ channel Deposited 2017-03-24	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–140（140 aa） Fragment：UNP residues 1-140,381-870,1006-1159 Chain A 381–870（490 aa） Fragment：UNP residues 1-140,381-870,1006-1159 Chain A 1006–1159（154 aa） Fragment：UNP residues 1-140,381-870,1006-1159	Mutation：S631A Mutation：S631A Mutation：S631A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；pH 7.4, adjusted with NaOH cryo-EM vitrification conditions Cryogen ETHANE；one blot: 3 second blot time, 0 blot force	Resolution 4.00 Å
8IO4 Herg1a-herg1b open state Deposited 2023-03-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–1159（1159 aa） Chain B 1–1159（1159 aa） Chain C 1–1159（1159 aa） Chain D 1–1159（1159 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
8ZYN Cryo-EM Structure of inhibitor-free hERG Channel Deposited 2024-06-18	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–140（140 aa） Chain A 351–870（520 aa） Chain A 1006–1159（154 aa） Chain B 1–140（140 aa） Chain B 351–870（520 aa） Chain B 1006–1159（154 aa） Chain C 1–140（140 aa） Chain C 351–870（520 aa） Chain C 1006–1159（154 aa） Chain D 1–140（140 aa） Chain D 351–870（520 aa） Chain D 1006–1159（154 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.27 Å
8ZYO Cryo-EM Structure of astemizole-bound hERG Channel Deposited 2024-06-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–140（140 aa） Chain A 351–870（520 aa） Chain A 1006–1159（154 aa） Chain B 1–140（140 aa） Chain B 351–870（520 aa） Chain B 1006–1159（154 aa） Chain C 1–140（140 aa） Chain C 351–870（520 aa） Chain C 1006–1159（154 aa） Chain D 1–140（140 aa） Chain D 351–870（520 aa） Chain D 1006–1159（154 aa）	Not recorded	XB7 1-[(4-fluorophenyl)methyl]-N-{1-[2-(4-methoxyphenyl)ethyl]piperidin-4-yl}-1H-benzimidazol-2-amine × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.29 Å
8ZYP Cryo-EM Structure of E-4031-bound hERG Channel Deposited 2024-06-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–140（140 aa） Chain A 351–870（520 aa） Chain A 1006–1159（154 aa） Chain B 1–140（140 aa） Chain B 351–870（520 aa） Chain B 1006–1159（154 aa） Chain C 1–140（140 aa） Chain C 351–870（520 aa） Chain C 1006–1159（154 aa） Chain D 1–140（140 aa） Chain D 351–870（520 aa） Chain D 1006–1159（154 aa）	Not recorded	A1L2J ~{N}-[4-[1-[2-(6-methylpyridin-2-yl)ethyl]piperidin-4-yl]carbonylphenyl]methanesulfonamide × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.19 Å
8ZYQ Cryo-EM Structure of pimozide-bound hERG Channel Deposited 2024-06-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–140（140 aa） Chain A 351–870（520 aa） Chain A 1006–1159（154 aa） Chain B 1–140（140 aa） Chain B 351–870（520 aa） Chain B 1006–1159（154 aa） Chain C 1–140（140 aa） Chain C 351–870（520 aa） Chain C 1006–1159（154 aa） Chain D 1–140（140 aa） Chain D 351–870（520 aa） Chain D 1006–1159（154 aa）	Not recorded	1II 3-[1-[4,4-bis(4-fluorophenyl)butyl]piperidin-4-yl]-1~{H}-benzimidazol-2-one × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.18 Å
9CHP Cryo-EM structure of the human ether-a-go-go related K+ channel (hERG) in 300 mM K+ Deposited 2024-07-01	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–1159（1159 aa） Chain B 1–1159（1159 aa） Chain C 1–1159（1159 aa） Chain D 1–1159（1159 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
9CHQ Cryo-EM structure of the human ether-a-go-go related K+ channel (hERG) in 3 mM K+ Deposited 2024-07-01	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–1159（1159 aa） Chain B 1–1159（1159 aa） Chain C 1–1159（1159 aa） Chain D 1–1159（1159 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
9CHR Cryo-EM structure of the human ether-a-go-go related K+ channel (hERG) in 300 mM K+ without symmetry Deposited 2024-07-01	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–1159（1159 aa） Chain B 1–1159（1159 aa） Chain C 1–1159（1159 aa） Chain D 1–1159（1159 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
9CHS Cryo-EM structure of the human ether-a-go-go related K+ channel (hERG) in 3 mM K+ without symmetry Deposited 2024-07-01	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–1159（1159 aa） Chain B 1–1159（1159 aa） Chain C 1–1159（1159 aa） Chain D 1–1159（1159 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å

20 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	KCNH2_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–135； UniProt 734–864

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	6syg
Deposition date deposition_date	2019-09-27
Structure title title	Crystal structure of the Cyclic Nucleotide-Binding Homology Domain of the human KCNH2 channel
Keywords keywords	Intracellular domain, CNBHD, hERG, 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	15.81 Å
Radius of gyration Rg (electron density) rg_electron	14.47 Å
Forward intensity I(0) i0	4272590.00
Molecular weight molecular_weight	14879.0 kDa
Excluded volume excluded_volume	18684 Å³
Envelope volume envelope_volume	20867 Å³
Hydration-shell volume shell_volume	12409 Å³
Envelope diameter envelope_diameter	50.5 Å
Shell Rg shell_rg	20.08 Å
Envelope Rg envelope_rg	14.73 Å
Shape Rg shape_rg	14.43 Å
Total Rg total_rg	15.72 Å
Total atoms total_atoms	1048
Residues n_residues	135
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	54.2 Å
Rg (real space) rg_real	15.73 Å
Rg uncertainty (real space) rg_real_error	0.41 Å
I(0) (real space) i0_real	4.2730e+06
I(0) uncertainty (real space) i0_real_error	4.9220e+04
Rg (reciprocal space) rg_reciprocal	15.74 Å
I(0) (reciprocal space) i0_reciprocal	4273000.0000
Solution quality estimate total_estimate	0.7908
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	49.4 Å
Skewness Skewness skewness	0.166
Kurtosis Kurtosis kurtosis	-0.359
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	629600.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.762; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.000

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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) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	6sygA00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	10 — Jelly Rolls

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8. Citations (1)

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Unit-cell length a length_a	57.493 Å
Unit-cell length b length_b	90.649 Å
Unit-cell length c length_c	61.111 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	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	orthorhombic

Resolution resolution	1.500 Å
Low-resolution limit resolution_low	48.550 Å
R factor r_factor	0.1706
R_work r_work	0.1702
R_free r_free	0.1840

Description description	Potassium voltage-gated channel subfamily H member 2
Molecular weight formula_weight	15066.4 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	1366

Crystal structure of the Cyclic Nucleotide-Binding Homology Domain of the human KCNH2 channel

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

Potassium voltage-gated channel subfamily H member 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) 1 domains

CATH v4.4 (1 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	297

fit	/app/data/saxs_computation/sy/6syg/6syg.fit
pddf	/app/data/pr_computation/sy/6syg/6syg.pr.out
profile	/app/data/saxs_computation/sy/6syg/6syg.dat