7ej2

human voltage-gated potassium channel KV1.3 H451N mutant

Method: ELECTRON MICROSCOPY Dmax: 163.1 Å Quality: GOOD

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

Voltage-gated potassium channel subunit beta-2

Homo sapiens

UniProt Q13303

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 heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–367 Chain C; UniProt 1–367 Chain E; UniProt 1–367 Chain G; UniProt 1–367 Not recorded Potassium voltage-gated channel subfamily A member 3 × 4 (P22001) NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KCAB2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–367; UniProt 1–367 Author chain C; PDBConstruct 1–367; UniProt 1–367 Author chain E; PDBConstruct 1–367; UniProt 1–367 Author chain G; PDBConstruct 1–367; UniProt 1–367

Potassium voltage-gated channel subfamily A member 3

Homo sapiens

UniProt P22001

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 heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 1–575 Chain D; UniProt 1–575 Chain F; UniProt 1–575 Chain H; UniProt 1–575 Mutation:H451N Voltage-gated potassium channel subunit beta-2 × 4 (Q13303) NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KCNA3_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–575; UniProt 1–575 Author chain D; PDBConstruct 1–575; UniProt 1–575 Author chain F; PDBConstruct 1–575; UniProt 1–575 Author chain H; PDBConstruct 1–575; UniProt 1–575

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 7ej2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7ej2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7ej2
Deposition date deposition_date2021-04-01
Structure title titlehuman voltage-gated potassium channel KV1.3 H451N mutant
Keywords keywordspotassium channel, complex, C-type inactivation, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier52.35
Radius of gyration Rg (electron density) rg_electron52.64
Forward intensity I(0) i01203930000.00
Molecular weight molecular_weight297290.0 kDa
Excluded volume excluded_volume374890 ų
Envelope volume envelope_volume563830 ų
Hydration-shell volume shell_volume89583 ų
Envelope diameter envelope_diameter163.9
Shell Rg shell_rg55.54
Envelope Rg envelope_rg51.78
Shape Rg shape_rg52.65
Total Rg total_rg52.70
Total atoms total_atoms20968
Residues n_residues2728
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax163.1
Rg (real space) rg_real52.35
Rg uncertainty (real space) rg_real_error1.64
I(0) (real space) i0_real1.2040e+09
I(0) uncertainty (real space) i0_real_error2.5520e+07
Rg (reciprocal space) rg_reciprocal52.34
I(0) (reciprocal space) i0_reciprocal1204000000.0000
Solution quality estimate total_estimate0.8494
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.8
Skewness Skewness skewness0.265
Kurtosis Kurtosis kurtosis-0.688
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha83550000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.920; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.279

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)