9vlg

Structure of human alpha-2/delta-1 with crisugabalin

Method: ELECTRON MICROSCOPY Dmax: 108.4 Å Quality: GOOD

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

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

Homo sapiens

UniProt P54289

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 Monomer Protein × 1 其他Polymer 4 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 25–1064 Not recorded beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 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 × 2 A1ESQ Crisugabalin × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.01 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.

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

View Construct and Data Evidence
UniProt name CA2D1_HUMAN
Isoform P54289-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 17–1064; UniProt 25–1064

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 9vlg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9vlg
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9vlg
Deposition date deposition_date2025-06-25
Structure title titleStructure of human alpha-2/delta-1 with crisugabalin
Keywords keywordsComplex, Alpha-2/delta-1, Crisugabalin, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier33.59
Radius of gyration Rg (electron density) rg_electron33.11
Forward intensity I(0) i0337801000.00
Molecular weight molecular_weight99014.0 kDa
Excluded volume excluded_volume95857 ų
Envelope volume envelope_volume168080 ų
Hydration-shell volume shell_volume42770 ų
Envelope diameter envelope_diameter111.0
Shell Rg shell_rg39.70
Envelope Rg envelope_rg32.64
Shape Rg shape_rg33.04
Total Rg total_rg33.58
Total atoms total_atoms7511
Residues n_residues910
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 dmax108.4
Rg (real space) rg_real33.59
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real3.3780e+08
I(0) uncertainty (real space) i0_real_error4.8080e+06
Rg (reciprocal space) rg_reciprocal33.59
I(0) (reciprocal space) i0_reciprocal337800000.0000
Solution quality estimate total_estimate0.8983
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.9
Skewness Skewness skewness0.300
Kurtosis Kurtosis kurtosis-0.577
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha69000000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.923; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.967; Smooth: 0.939

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)