9cx7

Native human GABAA receptor of beta3-alpha1-gamma2-beta3-alpha2 assembly

Method: ELECTRON MICROSCOPY Dmax: 131.1 Å Quality: GOOD

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

Gamma-aminobutyric acid receptor subunit beta-3

OrganismNot specified

UniProt P28472

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 × 7 其他Polymer 6 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 26–473 Chain D; UniProt 26–473 Not recorded Gamma-aminobutyric acid receptor subunit alpha-1 × 1 (P14867) Gamma-aminobutyric acid receptor subunit gamma-2 × 1 (P18507) Gamma-aminobutyric acid receptor subunit alpha-2 × 1 (P47869) IgG2b Fab_1F4 Heavy Chain × 1 Kappa Fab_1F4 Light Chain × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ;alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 ABU GAMMA-AMINO-BUTANOIC ACID × 2 PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;3.5 s Blot. Resolution 3.30 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.

94 other PDB entries and 94 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBRB3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–448; UniProt 26–473 Author chain D; PDBConstruct 1–448; UniProt 26–473

Gamma-aminobutyric acid receptor subunit alpha-1

OrganismNot specified

UniProt P14867

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 × 7 其他Polymer 6 PDB declaration: heptameric(7) Consistent with protein copy count Chain B; UniProt 28–456 Not recorded Gamma-aminobutyric acid receptor subunit beta-3 × 2 (P28472) Gamma-aminobutyric acid receptor subunit gamma-2 × 1 (P18507) Gamma-aminobutyric acid receptor subunit alpha-2 × 1 (P47869) IgG2b Fab_1F4 Heavy Chain × 1 Kappa Fab_1F4 Light Chain × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ;alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 ABU GAMMA-AMINO-BUTANOIC ACID × 2 PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;3.5 s Blot. Resolution 3.30 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.

83 other PDB entries and 85 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBRA1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–429; UniProt 28–456

Gamma-aminobutyric acid receptor subunit gamma-2

OrganismNot specified

UniProt P18507

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 × 7 其他Polymer 6 PDB declaration: heptameric(7) Consistent with protein copy count Chain C; UniProt 40–475 Not recorded Gamma-aminobutyric acid receptor subunit beta-3 × 2 (P28472) Gamma-aminobutyric acid receptor subunit alpha-1 × 1 (P14867) Gamma-aminobutyric acid receptor subunit alpha-2 × 1 (P47869) IgG2b Fab_1F4 Heavy Chain × 1 Kappa Fab_1F4 Light Chain × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ;alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 ABU GAMMA-AMINO-BUTANOIC ACID × 2 PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;3.5 s Blot. Resolution 3.30 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.

70 other PDB entries and 70 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBRG2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–436; UniProt 40–475

Gamma-aminobutyric acid receptor subunit alpha-2

OrganismNot specified

UniProt P47869

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 × 7 其他Polymer 6 PDB declaration: heptameric(7) Consistent with protein copy count Chain E; UniProt 29–451 Not recorded Gamma-aminobutyric acid receptor subunit beta-3 × 2 (P28472) Gamma-aminobutyric acid receptor subunit alpha-1 × 1 (P14867) Gamma-aminobutyric acid receptor subunit gamma-2 × 1 (P18507) IgG2b Fab_1F4 Heavy Chain × 1 Kappa Fab_1F4 Light Chain × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ;alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 ABU GAMMA-AMINO-BUTANOIC ACID × 2 PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;3.5 s Blot. Resolution 3.30 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBRA2_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 1–423; UniProt 29–451

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 9cx7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9cx7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9cx7
Deposition date deposition_date2024-07-30
Structure title titleNative human GABAA receptor of beta3-alpha1-gamma2-beta3-alpha2 assembly
Keywords keywordsIon channels, Heteropentamer, Receptor, Inhibitory., MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.63
Radius of gyration Rg (electron density) rg_electron40.29
Forward intensity I(0) i0592642000.00
Molecular weight molecular_weight206940.0 kDa
Excluded volume excluded_volume261860 ų
Envelope volume envelope_volume342860 ų
Hydration-shell volume shell_volume70283 ų
Envelope diameter envelope_diameter139.7
Shell Rg shell_rg46.51
Envelope Rg envelope_rg39.86
Shape Rg shape_rg40.29
Total Rg total_rg40.65
Total atoms total_atoms14573
Residues n_residues1755
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 dmax131.1
Rg (real space) rg_real40.54
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real5.9260e+08
I(0) uncertainty (real space) i0_real_error9.4150e+06
Rg (reciprocal space) rg_reciprocal40.63
I(0) (reciprocal space) i0_reciprocal592700000.0000
Solution quality estimate total_estimate0.8903
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.0
Skewness Skewness skewness0.262
Kurtosis Kurtosis kurtosis-0.453
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha62780000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.887; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.909

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

8. Citations (1)

9. Files and Curves (10)