9ouo

Native GABA-A receptor from rat cerebella, beta1-alpha1-beta1-alpha1-gamma2 subtype, in complex with GABA and PZ-II-029

Method: ELECTRON MICROSCOPY Dmax: 145.7 Å Quality: GOOD

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

Gamma-aminobutyric acid receptor subunit gamma-2

OrganismNot specified

UniProt P18508

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 × 9 其他Polymer 7 PDB declaration: nonameric(9) Consistent with protein copy count Chain D; UniProt 1–466 Not recorded 8E3 Fab heavy chain × 2 8E3 Fab light chain × 2 Gamma-aminobutyric acid receptor subunit alpha-1 × 2 (P62813) Gamma-aminobutyric acid receptor subunit beta-1 × 2 (P15431) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[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 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 A1CEP 7-methoxy-2-(4-methoxyphenyl)-1,2-dihydro-3H-pyrazolo[4,3-c]quinolin-3-one × 1 ABU GAMMA-AMINO-BUTANOIC ACID × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.92 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBRG2_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain D; PDBConstruct 1–466; UniProt 1–466

Gamma-aminobutyric acid receptor subunit alpha-1

OrganismNot specified

UniProt P62813

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 × 9 其他Polymer 7 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 1–455 Chain C; UniProt 1–455 Not recorded Gamma-aminobutyric acid receptor subunit gamma-2 × 1 (P18508) 8E3 Fab heavy chain × 2 8E3 Fab light chain × 2 Gamma-aminobutyric acid receptor subunit beta-1 × 2 (P15431) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[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 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 A1CEP 7-methoxy-2-(4-methoxyphenyl)-1,2-dihydro-3H-pyrazolo[4,3-c]quinolin-3-one × 1 ABU GAMMA-AMINO-BUTANOIC ACID × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.92 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBRA1_RAT
Isoform
PDB entities 4
Chains and sequence ranges Author chain A; PDBConstruct 1–455; UniProt 1–455 Author chain C; PDBConstruct 1–455; UniProt 1–455

Gamma-aminobutyric acid receptor subunit beta-1

OrganismNot specified

UniProt P15431

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 × 9 其他Polymer 7 PDB declaration: nonameric(9) Consistent with protein copy count Chain B; UniProt 1–474 Chain E; UniProt 1–474 Not recorded Gamma-aminobutyric acid receptor subunit gamma-2 × 1 (P18508) 8E3 Fab heavy chain × 2 8E3 Fab light chain × 2 Gamma-aminobutyric acid receptor subunit alpha-1 × 2 (P62813) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[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 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 A1CEP 7-methoxy-2-(4-methoxyphenyl)-1,2-dihydro-3H-pyrazolo[4,3-c]quinolin-3-one × 1 ABU GAMMA-AMINO-BUTANOIC ACID × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.92 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBRB1_RAT
Isoform
PDB entities 5
Chains and sequence ranges Author chain B; PDBConstruct 1–474; UniProt 1–474 Author chain E; PDBConstruct 1–474; UniProt 1–474

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 9ouo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ouo
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9ouo
Deposition date deposition_date2025-05-29
Structure title titleNative GABA-A receptor from rat cerebella, beta1-alpha1-beta1-alpha1-gamma2 subtype, in complex with GABA and PZ-II-029
Keywords keywordsneurotransmitter receptor, cys-loop receptor, ligand-gated ion channel, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.92
Radius of gyration Rg (electron density) rg_electron39.63
Forward intensity I(0) i0462798000.00
Molecular weight molecular_weight175130.0 kDa
Excluded volume excluded_volume218950 ų
Envelope volume envelope_volume295410 ų
Hydration-shell volume shell_volume63059 ų
Envelope diameter envelope_diameter157.1
Shell Rg shell_rg44.40
Envelope Rg envelope_rg39.40
Shape Rg shape_rg39.61
Total Rg total_rg39.99
Total atoms total_atoms24261
Residues n_residues1497
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 dmax145.7
Rg (real space) rg_real40.06
Rg uncertainty (real space) rg_real_error1.58
I(0) (real space) i0_real4.6280e+08
I(0) uncertainty (real space) i0_real_error8.4160e+06
Rg (reciprocal space) rg_reciprocal39.97
I(0) (reciprocal space) i0_reciprocal462800000.0000
Solution quality estimate total_estimate0.8251
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary47.3
Skewness Skewness skewness0.532
Kurtosis Kurtosis kurtosis0.140
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha86390000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.606; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.933

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)