9fg1

Cryo-EM structure of the alpha1beta3gamma2 GABA(A) receptor in complex with GABA and Nb38 in the short-lived asymmetric desensitised 2 state

Method: ELECTRON MICROSCOPY Dmax: 128.1 Å Quality: GOOD

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

Gamma-aminobutyric acid receptor subunit alpha-1

Homo sapiens

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 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 32–339 Chain A; UniProt 418–456 Chain D; UniProt 32–339 Chain D; UniProt 418–456 Not recorded Gamma-aminobutyric acid receptor subunit beta-3 × 2 (P28472) Isoform 1 of Gamma-aminobutyric acid receptor subunit gamma-2 × 1 (P18507) Nanobody38 × 2 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[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 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ;alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]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 D3D (19S,22R,25R)-22,25,26-trihydroxy-16,22-dioxo-17,21,23-trioxa-22lambda~5~-phosphahexacosan-19-yl (9E)-octadec-9-enoate × 2 D10 DECANE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;137 mM NaCl, 2.7 mM KCl, 4.3 mM Na2HPO 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.

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 1
Chains and sequence ranges Author chain A; PDBConstruct 58–365; UniProt 32–339 Author chain A; PDBConstruct 373–411; UniProt 418–456 Author chain D; PDBConstruct 58–365; UniProt 32–339 Author chain D; PDBConstruct 373–411; UniProt 418–456

Gamma-aminobutyric acid receptor subunit beta-3

Homo sapiens

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 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain B; UniProt 26–332 Chain B; UniProt 447–473 Chain E; UniProt 26–332 Chain E; UniProt 447–473 Not recorded Gamma-aminobutyric acid receptor subunit alpha-1 × 2 (P14867) Isoform 1 of Gamma-aminobutyric acid receptor subunit gamma-2 × 1 (P18507) Nanobody38 × 2 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[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 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ;alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]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 D3D (19S,22R,25R)-22,25,26-trihydroxy-16,22-dioxo-17,21,23-trioxa-22lambda~5~-phosphahexacosan-19-yl (9E)-octadec-9-enoate × 2 D10 DECANE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;137 mM NaCl, 2.7 mM KCl, 4.3 mM Na2HPO 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.

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 2
Chains and sequence ranges Author chain B; PDBConstruct 55–361; UniProt 26–332 Author chain B; PDBConstruct 369–395; UniProt 447–473 Author chain E; PDBConstruct 55–361; UniProt 26–332 Author chain E; PDBConstruct 369–395; UniProt 447–473

Isoform 1 of Gamma-aminobutyric acid receptor subunit gamma-2

Homo sapiens

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 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain C; UniProt 40–361 Chain C; UniProt 447–475 Not recorded Gamma-aminobutyric acid receptor subunit alpha-1 × 2 (P14867) Gamma-aminobutyric acid receptor subunit beta-3 × 2 (P28472) Nanobody38 × 2 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[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 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ;alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]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 D3D (19S,22R,25R)-22,25,26-trihydroxy-16,22-dioxo-17,21,23-trioxa-22lambda~5~-phosphahexacosan-19-yl (9E)-octadec-9-enoate × 2 D10 DECANE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;137 mM NaCl, 2.7 mM KCl, 4.3 mM Na2HPO 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.

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 P18507-2
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 3–324; UniProt 40–361 Author chain C; PDBConstruct 331–359; UniProt 447–475

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 9fg1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9fg1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9fg1
Deposition date deposition_date2024-05-23
Structure title titleCryo-EM structure of the alpha1beta3gamma2 GABA(A) receptor in complex with GABA and Nb38 in the short-lived asymmetric desensitised 2 state
Keywords keywordsGABA, neurotransmission, gating cycle, time-resolved cryo-EM, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.08
Radius of gyration Rg (electron density) rg_electron39.57
Forward intensity I(0) i0711606000.00
Molecular weight molecular_weight228190.0 kDa
Excluded volume excluded_volume289250 ų
Envelope volume envelope_volume373150 ų
Hydration-shell volume shell_volume76002 ų
Envelope diameter envelope_diameter134.8
Shell Rg shell_rg47.21
Envelope Rg envelope_rg39.21
Shape Rg shape_rg39.59
Total Rg total_rg39.89
Total atoms total_atoms16080
Residues n_residues1921
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 dmax128.1
Rg (real space) rg_real39.94
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real7.1160e+08
I(0) uncertainty (real space) i0_real_error1.2160e+07
Rg (reciprocal space) rg_reciprocal40.08
I(0) (reciprocal space) i0_reciprocal711700000.0000
Solution quality estimate total_estimate0.8899
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary49.3
Skewness Skewness skewness0.214
Kurtosis Kurtosis kurtosis-0.426
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha110500000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.890; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.905

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)