6dw0

Cryo-EM structure of the benzodiazepine-sensitive alpha1beta1gamma2S tri-heteromeric GABAA receptor in complex with GABA (Whole map)

Method: ELECTRON MICROSCOPY Dmax: 118.2 Å Quality: GOOD

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

Gamma-aminobutyric acid receptor subunit gamma-2

Rattus norvegicus

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 × 5 其他Polymer 6 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 1–466 Fragment:residues 63-361 Gamma-aminobutyric acid receptor subunit alpha-1,Gamma-aminobutyric acid receptor subunit alpha-1 × 2 (P62813) Gamma-aminobutyric acid receptor subunit beta-1,Gamma-aminobutyric acid receptor subunit beta-1 × 2 (P15431) ;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 ; × 1 ;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 × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ABU GAMMA-AMINO-BUTANOIC ACID × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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,Gamma-aminobutyric acid receptor subunit alpha-1

Rattus norvegicus

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 × 5 其他Polymer 6 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–340 Chain A; UniProt 409–455 Chain C; UniProt 1–340 Chain C; UniProt 409–455 Fragment:residues 39-334 Gamma-aminobutyric acid receptor subunit gamma-2 × 1 (P18508) Gamma-aminobutyric acid receptor subunit beta-1,Gamma-aminobutyric acid receptor subunit beta-1 × 2 (P15431) ;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 ; × 1 ;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 × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ABU GAMMA-AMINO-BUTANOIC ACID × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 2
Chains and sequence ranges Author chain A; PDBConstruct 1–340; UniProt 1–340 Author chain A; PDBConstruct 342–388; UniProt 409–455 Author chain C; PDBConstruct 1–340; UniProt 1–340 Author chain C; PDBConstruct 342–388; UniProt 409–455

Gamma-aminobutyric acid receptor subunit beta-1,Gamma-aminobutyric acid receptor subunit beta-1

Rattus norvegicus

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 × 5 其他Polymer 6 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 1–333 Chain B; UniProt 440–474 Chain E; UniProt 1–333 Chain E; UniProt 440–474 Fragment:residues 33-474 Gamma-aminobutyric acid receptor subunit gamma-2 × 1 (P18508) Gamma-aminobutyric acid receptor subunit alpha-1,Gamma-aminobutyric acid receptor subunit alpha-1 × 2 (P62813) ;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 ; × 1 ;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 × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ABU GAMMA-AMINO-BUTANOIC ACID × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 3
Chains and sequence ranges Author chain B; PDBConstruct 1–333; UniProt 1–333 Author chain B; PDBConstruct 336–370; UniProt 440–474 Author chain E; PDBConstruct 1–333; UniProt 1–333 Author chain E; PDBConstruct 336–370; UniProt 440–474

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 6dw0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6dw0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6dw0
Deposition date deposition_date2018-06-26
Structure title titleCryo-EM structure of the benzodiazepine-sensitive alpha1beta1gamma2S tri-heteromeric GABAA receptor in complex with GABA (Whole map)
Keywords keywordsNeurotransmission, GABA Receptors, GABA, Cys Loop Receptors, 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_guinier36.65
Radius of gyration Rg (electron density) rg_electron36.15
Forward intensity I(0) i0417412000.00
Molecular weight molecular_weight169440.0 kDa
Excluded volume excluded_volume213740 ų
Envelope volume envelope_volume291380 ų
Hydration-shell volume shell_volume65291 ų
Envelope diameter envelope_diameter121.5
Shell Rg shell_rg43.85
Envelope Rg envelope_rg35.80
Shape Rg shape_rg36.18
Total Rg total_rg36.58
Total atoms total_atoms11929
Residues n_residues1529
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 dmax118.2
Rg (real space) rg_real36.53
Rg uncertainty (real space) rg_real_error1.05
I(0) (real space) i0_real4.1740e+08
I(0) uncertainty (real space) i0_real_error6.9990e+06
Rg (reciprocal space) rg_reciprocal36.61
I(0) (reciprocal space) i0_reciprocal417400000.0000
Solution quality estimate total_estimate0.8776
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.8
Skewness Skewness skewness0.293
Kurtosis Kurtosis kurtosis-0.278
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha146200000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.847; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.871

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)