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2n7g

Structure of the cyclic nucleotide-binding homology domain of the hERG channel

Method: SOLUTION NMR Dmax: 54.7 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Potassium voltage-gated channel subfamily H member 2

Homo sapiens

UniProt Q12809

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 Fragment：UNP residues 734-869 No other associated polymer 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

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 2N7G 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 method 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 conditions 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 conditions 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 conditions 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 conditions 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
4HP9 Crystal structure of the N-terminal truncated PAS domain from the hERG potassium channel Deposited 2012-10-23 Different construct Different experimental method 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 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：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
6SYG Crystal structure of the Cyclic Nucleotide-Binding Homology Domain of the human KCNH2 channel Deposited 2019-09-27 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）
Not recorded No recorded non-water small molecule 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
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 24–154； 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.

SAXS scattering curve SAXS Profile

SAXS profile for 2n7g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2n7g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2n7g
Deposition date deposition_date2015-09-10
Structure title titleStructure of the cyclic nucleotide-binding homology domain of the hERG channel
Keywords keywordshERG, CNBHD, ion channel, LQTS2, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier15.38 Å
Radius of gyration Rg (electron density) rg_electron14.88 Å
Forward intensity I(0) i01156130000.00
Molecular weight molecular_weight294220.0 kDa
Excluded volume excluded_volume370480 ų
Envelope volume envelope_volume34543 ų
Hydration-shell volume shell_volume16943 ų
Envelope diameter envelope_diameter61.3 Å
Shell Rg shell_rg23.30 Å
Envelope Rg envelope_rg17.55 Å
Shape Rg shape_rg14.82 Å
Total Rg total_rg15.21 Å
Total atoms total_atoms41520
Residues n_residues2620
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax54.7 Å
Rg (real space) rg_real15.30 Å
Rg uncertainty (real space) rg_real_error0.37 Å
I(0) (real space) i0_real1.1560e+09
I(0) uncertainty (real space) i0_real_error1.3770e+07
Rg (reciprocal space) rg_reciprocal15.31 Å
I(0) (reciprocal space) i0_reciprocal1156000000.0000
Solution quality estimate total_estimate0.8449
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.7 Å
Skewness Skewness skewness0.134
Kurtosis Kurtosis kurtosis-0.343
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha310000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.665; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.997
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2n7gA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily10 — Jelly Rolls
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8. Citations (1)

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9. Files and Curves (10)