6ebl

The voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs, cytosolic domain

Method: ELECTRON MICROSCOPY Dmax: 118.9 Å Quality: GOOD

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

Voltage-gated potassium channel subunit beta-2

Rattus norvegicus

UniProt P62483

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 Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 37–367 Chain C; UniProt 37–367 Chain E; UniProt 37–367 Chain G; UniProt 37–367 Mutation:cytosolic domain (UNP residues 37-367) Potassium voltage-gated channel subfamily A member 2,Potassium voltage-gated channel subfamily B member 2 chimera × 4 (P63142,Q63099) NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4 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 3.00 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.

17 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KCAB2_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–333; UniProt 37–367 Author chain C; PDBConstruct 3–333; UniProt 37–367 Author chain E; PDBConstruct 3–333; UniProt 37–367 Author chain G; PDBConstruct 3–333; UniProt 37–367

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 Heteromer Protein × 8 PDB declaration: octameric(8) 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 Voltage-gated potassium channel subunit beta-2 × 4 (P62483) NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4 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 3.00 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 2
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 Heteromer Protein × 8 PDB declaration: octameric(8) 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 Voltage-gated potassium channel subunit beta-2 × 4 (P62483) NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4 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 3.00 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 2
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 6ebl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6ebl
Deposition date deposition_date2018-08-06
Structure title titleThe voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs, cytosolic domain
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_guinier38.77
Radius of gyration Rg (electron density) rg_electron37.89
Forward intensity I(0) i0582568000.00
Molecular weight molecular_weight196840.0 kDa
Excluded volume excluded_volume246180 ų
Envelope volume envelope_volume316240 ų
Hydration-shell volume shell_volume66819 ų
Envelope diameter envelope_diameter126.5
Shell Rg shell_rg45.67
Envelope Rg envelope_rg38.05
Shape Rg shape_rg37.87
Total Rg total_rg38.38
Total atoms total_atoms13824
Residues n_residues1708
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 dmax118.9
Rg (real space) rg_real38.50
Rg uncertainty (real space) rg_real_error0.61
I(0) (real space) i0_real5.8260e+08
I(0) uncertainty (real space) i0_real_error8.6940e+06
Rg (reciprocal space) rg_reciprocal38.67
I(0) (reciprocal space) i0_reciprocal582700000.0000
Solution quality estimate total_estimate0.8879
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary55.1
Skewness Skewness skewness0.093
Kurtosis Kurtosis kurtosis-0.461
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha171100000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.917; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.811

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_idd6ebla_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamilyc.1.7 — NAD(P)-linked oxidoreductase
Family Family familyc.1.7.1 — Aldo-keto reductases (NADP)
Domain ID domain_idd6eblb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.42 — POZ domain
Superfamily Superfamily superfamilyd.42.1 — POZ domain
Family Family familyd.42.1.0 — automated matches
Domain ID domain_idd6eblc_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamilyc.1.7 — NAD(P)-linked oxidoreductase
Family Family familyc.1.7.1 — Aldo-keto reductases (NADP)
Domain ID domain_idd6ebld_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.42 — POZ domain
Superfamily Superfamily superfamilyd.42.1 — POZ domain
Family Family familyd.42.1.0 — automated matches
Domain ID domain_idd6eble_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamilyc.1.7 — NAD(P)-linked oxidoreductase
Family Family familyc.1.7.1 — Aldo-keto reductases (NADP)
Domain ID domain_idd6eblf_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.42 — POZ domain
Superfamily Superfamily superfamilyd.42.1 — POZ domain
Family Family familyd.42.1.0 — automated matches
Domain ID domain_idd6eblg_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamilyc.1.7 — NAD(P)-linked oxidoreductase
Family Family familyc.1.7.1 — Aldo-keto reductases (NADP)
Domain ID domain_idd6eblh_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.42 — POZ domain
Superfamily Superfamily superfamilyd.42.1 — POZ domain
Family Family familyd.42.1.0 — automated matches

CATH v4.4 (8 domains)

Domain ID domain_id6eblA00
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily100 — NADP-dependent oxidoreductase domain
Domain ID domain_id6eblB00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology710 — Potassium Channel Kv1.1; Chain A
Homologous superfamily homologous superfamily10 — Potassium Channel Kv1.1; Chain A
Domain ID domain_id6eblC00
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily100 — NADP-dependent oxidoreductase domain
Domain ID domain_id6eblD00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology710 — Potassium Channel Kv1.1; Chain A
Homologous superfamily homologous superfamily10 — Potassium Channel Kv1.1; Chain A
Domain ID domain_id6eblE00
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily100 — NADP-dependent oxidoreductase domain
Domain ID domain_id6eblF00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology710 — Potassium Channel Kv1.1; Chain A
Homologous superfamily homologous superfamily10 — Potassium Channel Kv1.1; Chain A
Domain ID domain_id6eblG00
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily100 — NADP-dependent oxidoreductase domain
Domain ID domain_id6eblH00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology710 — Potassium Channel Kv1.1; Chain A
Homologous superfamily homologous superfamily10 — Potassium Channel Kv1.1; Chain A

8. Citations (1)

9. Files and Curves (10)