8dd2

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

Method: ELECTRON MICROSCOPY Dmax: 142.6 Å Quality: GOOD

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 5 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 25–331 Chain A; UniProt 486–511 Chain C; UniProt 25–331 Chain C; UniProt 486–511 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 × 3 ;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 × 2 R5R Zolpidem × 3 ABU GAMMA-AMINO-BUTANOIC ACID × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;3.5 second blot Resolution 2.90 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
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–307; UniProt 25–331 Author chain A; PDBConstruct 315–340; UniProt 486–511 Author chain C; PDBConstruct 1–307; UniProt 25–331 Author chain C; PDBConstruct 315–340; UniProt 486–511

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 5 PDB declaration: nonameric(9) Consistent with protein copy count Chain B; UniProt 28–339 Chain D; UniProt 28–339 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 × 3 ;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 × 2 R5R Zolpidem × 3 ABU GAMMA-AMINO-BUTANOIC ACID × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;3.5 second blot Resolution 2.90 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 D; PDBConstruct 1–312; UniProt 28–339

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 5 PDB declaration: nonameric(9) Consistent with protein copy count Chain E; UniProt 40–361 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 × 3 ;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 × 2 R5R Zolpidem × 3 ABU GAMMA-AMINO-BUTANOIC ACID × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;3.5 second blot Resolution 2.90 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 38–359; UniProt 40–361

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 8dd2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8dd2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8dd2
Deposition date deposition_date2022-06-17
Structure title titleHuman GABAA receptor alpha1-beta2-gamma2 subtype in complex with GABA plus Zolpidem
Keywords keywordsGABAA receptor, Zolpidem, MEMBRANE PROTEIN-IMMUNE SYSTEM complex; MEMBRANE PROTEIN/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.09
Radius of gyration Rg (electron density) rg_electron42.72
Forward intensity I(0) i0832089000.00
Molecular weight molecular_weight247740.0 kDa
Excluded volume excluded_volume313820 ų
Envelope volume envelope_volume399970 ų
Hydration-shell volume shell_volume77575 ų
Envelope diameter envelope_diameter156.6
Shell Rg shell_rg48.22
Envelope Rg envelope_rg42.43
Shape Rg shape_rg42.73
Total Rg total_rg42.94
Total atoms total_atoms17459
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 dmax142.6
Rg (real space) rg_real42.98
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real8.3210e+08
I(0) uncertainty (real space) i0_real_error1.3660e+07
Rg (reciprocal space) rg_reciprocal43.09
I(0) (reciprocal space) i0_reciprocal832200000.0000
Solution quality estimate total_estimate0.8916
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary50.1
Skewness Skewness skewness0.235
Kurtosis Kurtosis kurtosis-0.494
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha88580000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.877; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.960

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id8dd2I01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8dd2J01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8dd2K01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8dd2L01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)