8fd7

Structure of the human L-type voltage-gated calcium channel Cav1.2 complexed with gabapentin

Method: ELECTRON MICROSCOPY Dmax: 202.3 Å Quality: REASONABLE

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

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

Oryctolagus cuniculus

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 × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 1–1106 Not recorded Voltage-dependent L-type calcium channel subunit alpha-1C × 1 (Q13936) Voltage-dependent L-type calcium channel subunit beta-3 × 1 (P54286) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 GBN [1-(AMINOMETHYL)CYCLOHEXYL]ACETIC ACID × 1 CA CALCIUM ION × 3 NA SODIUM ION × 1 WO9 (2R)-3-{[(R)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(dodecanoyloxy)propyl heptadecanoate × 1 YSW (2S)-3-{[(R)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(dodecanoyloxy)propyl dodecanoate × 1 CLR CHOLESTEROL × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 1
Chains and sequence ranges Author chain D; PDBConstruct 1–1105; UniProt 1–1106

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

Homo sapiens

UniProt Q13936

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 × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain K; UniProt 1–1648 Not recorded Voltage-dependent calcium channel subunit alpha-2/delta-1 × 1 (P13806) Voltage-dependent L-type calcium channel subunit beta-3 × 1 (P54286) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 GBN [1-(AMINOMETHYL)CYCLOHEXYL]ACETIC ACID × 1 CA CALCIUM ION × 3 NA SODIUM ION × 1 WO9 (2R)-3-{[(R)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(dodecanoyloxy)propyl heptadecanoate × 1 YSW (2S)-3-{[(R)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(dodecanoyloxy)propyl dodecanoate × 1 CLR CHOLESTEROL × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

23 other PDB entries and 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAC1C_HUMAN
Isoform Q13936-20
PDB entities 2
Chains and sequence ranges Author chain K; PDBConstruct 1–1648; UniProt 1–1648

Voltage-dependent L-type calcium channel subunit beta-3

Oryctolagus cuniculus

UniProt P54286

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 × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–477 Not recorded Voltage-dependent calcium channel subunit alpha-2/delta-1 × 1 (P13806) Voltage-dependent L-type calcium channel subunit alpha-1C × 1 (Q13936) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 GBN [1-(AMINOMETHYL)CYCLOHEXYL]ACETIC ACID × 1 CA CALCIUM ION × 3 NA SODIUM ION × 1 WO9 (2R)-3-{[(R)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(dodecanoyloxy)propyl heptadecanoate × 1 YSW (2S)-3-{[(R)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(dodecanoyloxy)propyl dodecanoate × 1 CLR CHOLESTEROL × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 CACB3_RABIT
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–477; UniProt 1–477

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 8fd7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8fd7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8fd7
Deposition date deposition_date2022-12-02
Structure title titleStructure of the human L-type voltage-gated calcium channel Cav1.2 complexed with gabapentin
Keywords keywordsvoltage-gated calcium channel, CaV alpha2delta, drug binding, gabapentin, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier56.19
Radius of gyration Rg (electron density) rg_electron56.25
Forward intensity I(0) i01016470000.00
Molecular weight molecular_weight279660.0 kDa
Excluded volume excluded_volume355700 ų
Envelope volume envelope_volume541650 ų
Hydration-shell volume shell_volume84597 ų
Envelope diameter envelope_diameter211.6
Shell Rg shell_rg54.07
Envelope Rg envelope_rg55.80
Shape Rg shape_rg56.23
Total Rg total_rg56.23
Total atoms total_atoms19698
Residues n_residues2416
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 dmax202.3
Rg (real space) rg_real56.60
Rg uncertainty (real space) rg_real_error2.68
I(0) (real space) i0_real1.0160e+09
I(0) uncertainty (real space) i0_real_error2.3290e+07
Rg (reciprocal space) rg_reciprocal55.85
I(0) (reciprocal space) i0_reciprocal1015000000.0000
Solution quality estimate total_estimate0.6190
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary57.8
Skewness Skewness skewness0.556
Kurtosis Kurtosis kurtosis-0.061
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha69950000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.756; Stabil: 1.000; Sysdev: 0.041; Positv: 1.000; Valcen: 0.933; Smooth: 0.718

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

8. Citations (1)

9. Files and Curves (10)