6ebm

The voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs, transmembrane domain of subunit alpha

Method: ELECTRON MICROSCOPY Dmax: 110.5 Å Quality: GOOD

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

Potassium voltage-gated channel subfamily A member 2,Potassium voltage-gated channel subfamily B member 2 chimera

Rattus norvegicus

UniProt P63142

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–266 Chain B; UniProt 303–499 Chain D; UniProt 1–266 Chain D; UniProt 303–499 Chain F; UniProt 1–266 Chain F; UniProt 303–499 Chain H; UniProt 1–266 Chain H; UniProt 303–499 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;A 3 microliter sample was applied to a plasma-cleaned grid and blotted for 10 seconds. Resolution 4.00 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.

16 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KCNA2_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 19–284; UniProt 1–266 Author chain B; PDBConstruct 317–513; UniProt 303–499 Author chain D; PDBConstruct 19–284; UniProt 1–266 Author chain D; PDBConstruct 317–513; UniProt 303–499 Author chain F; PDBConstruct 19–284; UniProt 1–266 Author chain F; PDBConstruct 317–513; UniProt 303–499 Author chain H; PDBConstruct 19–284; UniProt 1–266 Author chain H; PDBConstruct 317–513; UniProt 303–499

Potassium voltage-gated channel subfamily A member 2,Potassium voltage-gated channel subfamily B member 2 chimera

Rattus norvegicus

UniProt Q63099

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 278–309 Chain D; UniProt 278–309 Chain F; UniProt 278–309 Chain H; UniProt 278–309 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;A 3 microliter sample was applied to a plasma-cleaned grid and blotted for 10 seconds. Resolution 4.00 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.

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

View Construct and Data Evidence
UniProt name KCNB2_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 285–316; UniProt 278–309 Author chain D; PDBConstruct 285–316; UniProt 278–309 Author chain F; PDBConstruct 285–316; UniProt 278–309 Author chain H; PDBConstruct 285–316; UniProt 278–309

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 6ebm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6ebm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6ebm
Deposition date deposition_date2018-08-06
Structure title titleThe voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs, transmembrane domain of subunit alpha
Keywords keywordsMEMBRANE PROTEIN, transport protein, potassium channel, lipid nanodisc; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.98
Radius of gyration Rg (electron density) rg_electron34.64
Forward intensity I(0) i0195841000.00
Molecular weight molecular_weight120240.0 kDa
Excluded volume excluded_volume153410 ų
Envelope volume envelope_volume216770 ų
Hydration-shell volume shell_volume50916 ų
Envelope diameter envelope_diameter114.3
Shell Rg shell_rg42.12
Envelope Rg envelope_rg34.91
Shape Rg shape_rg34.75
Total Rg total_rg34.84
Total atoms total_atoms8532
Residues n_residues1192
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 dmax110.5
Rg (real space) rg_real35.77
Rg uncertainty (real space) rg_real_error0.65
I(0) (real space) i0_real1.9580e+08
I(0) uncertainty (real space) i0_real_error2.9890e+06
Rg (reciprocal space) rg_reciprocal35.91
I(0) (reciprocal space) i0_reciprocal195900000.0000
Solution quality estimate total_estimate0.8888
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.7
Skewness Skewness skewness0.113
Kurtosis Kurtosis kurtosis-0.388
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21240000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.900; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.868

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)