6jp8

Rabbit Cav1.1-Bay K8644 Complex

Method: ELECTRON MICROSCOPY Dmax: 199.6 Å Quality: GOOD

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

Voltage-dependent calcium channel gamma-1 subunit

OrganismNot specified

UniProt P19518

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 5 其他Polymer 7 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 1–222 Not recorded Voltage-dependent L-type calcium channel subunit beta-1 × 2 (P19517) Voltage-dependent L-type calcium channel subunit alpha-1S × 1 (P07293) Voltage-dependent calcium channel subunit alpha-2/delta-1 × 1 (P13806) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 C8U methyl (4~{S})-2,6-dimethyl-5-nitro-4-[2-(trifluoromethyl)phenyl]-1,4-dihydropyridine-3-carboxylate × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 CA CALCIUM ION × 2 ETA ETHANOLAMINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCG1_RABIT
Isoform
PDB entities 1
Chains and sequence ranges Author chain E; PDBConstruct 1–222; UniProt 1–222

Voltage-dependent L-type calcium channel subunit beta-1

Oryctolagus cuniculus

UniProt P19517

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 5 其他Polymer 7 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 80–524 Chain C; UniProt 80–524 Not recorded Voltage-dependent calcium channel gamma-1 subunit × 1 (P19518) Voltage-dependent L-type calcium channel subunit alpha-1S × 1 (P07293) Voltage-dependent calcium channel subunit alpha-2/delta-1 × 1 (P13806) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 C8U methyl (4~{S})-2,6-dimethyl-5-nitro-4-[2-(trifluoromethyl)phenyl]-1,4-dihydropyridine-3-carboxylate × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 CA CALCIUM ION × 2 ETA ETHANOLAMINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

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

View Construct and Data Evidence
UniProt name CACB1_RABIT
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 6–450; UniProt 80–524 Author chain C; PDBConstruct 6–450; UniProt 80–524

Voltage-dependent L-type calcium channel subunit alpha-1S

OrganismNot specified

UniProt P07293

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 5 其他Polymer 7 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–1873 Not recorded Voltage-dependent calcium channel gamma-1 subunit × 1 (P19518) Voltage-dependent L-type calcium channel subunit beta-1 × 2 (P19517) Voltage-dependent calcium channel subunit alpha-2/delta-1 × 1 (P13806) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 C8U methyl (4~{S})-2,6-dimethyl-5-nitro-4-[2-(trifluoromethyl)phenyl]-1,4-dihydropyridine-3-carboxylate × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 CA CALCIUM ION × 2 ETA ETHANOLAMINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

18 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAC1S_RABIT
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–1873; UniProt 1–1873

Voltage-dependent calcium channel subunit alpha-2/delta-1

OrganismNot specified

UniProt P13806

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 5 其他Polymer 7 PDB declaration: pentameric(5) Consistent with protein copy count Chain F; UniProt 29–1075 Not recorded Voltage-dependent calcium channel gamma-1 subunit × 1 (P19518) Voltage-dependent L-type calcium channel subunit beta-1 × 2 (P19517) Voltage-dependent L-type calcium channel subunit alpha-1S × 1 (P07293) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 C8U methyl (4~{S})-2,6-dimethyl-5-nitro-4-[2-(trifluoromethyl)phenyl]-1,4-dihydropyridine-3-carboxylate × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 CA CALCIUM ION × 2 ETA ETHANOLAMINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CA2D1_RABIT
Isoform
PDB entities 4
Chains and sequence ranges Author chain F; PDBConstruct 1–1046; UniProt 29–1075

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 6jp8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6jp8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6jp8
Deposition date deposition_date2019-03-26
Structure title titleRabbit Cav1.1-Bay K8644 Complex
Keywords keywordsMembrane protein complex modulated by FDA approved drug., MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier56.81
Radius of gyration Rg (electron density) rg_electron56.86
Forward intensity I(0) i01264780000.00
Molecular weight molecular_weight309400.0 kDa
Excluded volume excluded_volume392060 ų
Envelope volume envelope_volume606640 ų
Hydration-shell volume shell_volume92440 ų
Envelope diameter envelope_diameter213.3
Shell Rg shell_rg55.66
Envelope Rg envelope_rg56.63
Shape Rg shape_rg56.87
Total Rg total_rg56.78
Total atoms total_atoms21793
Residues n_residues2694
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 dmax199.6
Rg (real space) rg_real57.18
Rg uncertainty (real space) rg_real_error2.35
I(0) (real space) i0_real1.2650e+09
I(0) uncertainty (real space) i0_real_error2.7530e+07
Rg (reciprocal space) rg_reciprocal56.49
I(0) (reciprocal space) i0_reciprocal1263000000.0000
Solution quality estimate total_estimate0.8435
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary64.2
Skewness Skewness skewness0.553
Kurtosis Kurtosis kurtosis0.014
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha110200000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.801; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.964; Smooth: 0.596

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id6jp8B00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily40 — SH3 Domains
Domain ID domain_id6jp8C00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id6jp8E00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily150

8. Citations (1)

9. Files and Curves (10)