6x3w

Human GABAA receptor alpha1-beta2-gamma2 subtype in complex with GABA plus phenobarbital

Method: ELECTRON MICROSCOPY Dmax: 138.1 Å Quality: REASONABLE

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

Gamma-aminobutyric acid receptor subunit beta-2

Homo sapiens

UniProt P47870

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 4 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 25–331 Chain A; UniProt 487–512 Chain C; UniProt 25–331 Chain C; UniProt 487–512 Not recorded Gamma-aminobutyric acid receptor subunit alpha-1 × 2 (P14867) Gamma-aminobutyric acid receptor subunit gamma-2 × 1 (P18507) Kappa Fab Light Chain × 2 IgG2b Fab Heavy Chain × 2 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-(1-2)-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 × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ABU GAMMA-AMINO-BUTANOIC ACID × 2 UQA 5-ethyl-5-phenylpyrimidine-2,4,6(1H,3H,5H)-trione × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;3.5 second 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.

30 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBRB2_HUMAN
Isoform P47870-1
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–307; UniProt 25–331 Author chain A; PDBConstruct 316–341; UniProt 487–512 Author chain C; PDBConstruct 1–307; UniProt 25–331 Author chain C; PDBConstruct 316–341; UniProt 487–512

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 × 9 其他Polymer 4 PDB declaration: nonameric(9) Consistent with protein copy count Chain B; UniProt 28–339 Chain B; UniProt 418–456 Chain D; UniProt 28–339 Chain D; UniProt 418–456 Not recorded Gamma-aminobutyric acid receptor subunit beta-2 × 2 (P47870) Gamma-aminobutyric acid receptor subunit gamma-2 × 1 (P18507) Kappa Fab Light Chain × 2 IgG2b Fab Heavy Chain × 2 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-(1-2)-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 × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ABU GAMMA-AMINO-BUTANOIC ACID × 2 UQA 5-ethyl-5-phenylpyrimidine-2,4,6(1H,3H,5H)-trione × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;3.5 second 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 1–312; UniProt 28–339 Author chain B; PDBConstruct 320–358; UniProt 418–456 Author chain D; PDBConstruct 1–312; UniProt 28–339 Author chain D; PDBConstruct 320–358; UniProt 418–456

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 × 9 其他Polymer 4 PDB declaration: nonameric(9) Consistent with protein copy count Chain E; UniProt 42–361 Not recorded Gamma-aminobutyric acid receptor subunit beta-2 × 2 (P47870) Gamma-aminobutyric acid receptor subunit alpha-1 × 2 (P14867) Kappa Fab Light Chain × 2 IgG2b Fab Heavy Chain × 2 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-(1-2)-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 × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ABU GAMMA-AMINO-BUTANOIC ACID × 2 UQA 5-ethyl-5-phenylpyrimidine-2,4,6(1H,3H,5H)-trione × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;3.5 second 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 E; PDBConstruct 40–359; UniProt 42–361

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 6x3w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6x3w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6x3w
Deposition date deposition_date2020-05-21
Structure title titleHuman GABAA receptor alpha1-beta2-gamma2 subtype in complex with GABA plus phenobarbital
Keywords keywordsIon channel, Cys-loop receptor, pentametic ligand gated channel, GABAA receptor, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.81
Radius of gyration Rg (electron density) rg_electron42.43
Forward intensity I(0) i0829197000.00
Molecular weight molecular_weight246920.0 kDa
Excluded volume excluded_volume312640 ų
Envelope volume envelope_volume397480 ų
Hydration-shell volume shell_volume77212 ų
Envelope diameter envelope_diameter154.8
Shell Rg shell_rg48.14
Envelope Rg envelope_rg42.32
Shape Rg shape_rg42.44
Total Rg total_rg42.66
Total atoms total_atoms17399
Residues n_residues2121
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 dmax138.1
Rg (real space) rg_real42.70
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real8.2920e+08
I(0) uncertainty (real space) i0_real_error1.2650e+07
Rg (reciprocal space) rg_reciprocal42.81
I(0) (reciprocal space) i0_reciprocal829300000.0000
Solution quality estimate total_estimate0.6849
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.5
Skewness Skewness skewness0.233
Kurtosis Kurtosis kurtosis-0.497
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha87780000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.909; Stabil: 1.000; Sysdev: 0.083; Positv: 1.000; Valcen: 0.992; Smooth: 0.930

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)