9fex

Cryo-EM structure of the beta3 homomeric GABA(A) receptor in complex with HSM in the short-lived symmetric bound-closed state (C5)

Method: ELECTRON MICROSCOPY Dmax: 129.2 Å Quality: GOOD

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

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 Homooligomer Protein × 5 其他Polymer 10 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 26–332 Chain A; UniProt 447–473 Chain B; UniProt 26–332 Chain B; UniProt 447–473 Chain C; UniProt 26–332 Chain C; UniProt 447–473 Chain D; UniProt 26–332 Chain D; UniProt 447–473 Chain E; UniProt 26–332 Chain E; UniProt 447–473 Not recorded ;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 ; × 5 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 HSM HISTAMINE × 5 CL CHLORIDE ION × 5 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 2.60 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 1
Chains and sequence ranges Author chain A; PDBConstruct 55–361; UniProt 26–332 Author chain A; PDBConstruct 369–395; UniProt 447–473 Author chain B; PDBConstruct 55–361; UniProt 26–332 Author chain B; PDBConstruct 369–395; UniProt 447–473 Author chain C; PDBConstruct 55–361; UniProt 26–332 Author chain C; PDBConstruct 369–395; UniProt 447–473 Author chain D; PDBConstruct 55–361; UniProt 26–332 Author chain D; PDBConstruct 369–395; UniProt 447–473 Author chain E; PDBConstruct 55–361; UniProt 26–332 Author chain E; PDBConstruct 369–395; UniProt 447–473

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 9fex

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9fex
Deposition date deposition_date2024-05-21
Structure title titleCryo-EM structure of the beta3 homomeric GABA(A) receptor in complex with HSM in the short-lived symmetric bound-closed state (C5)
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_guinier38.54
Radius of gyration Rg (electron density) rg_electron38.20
Forward intensity I(0) i0543507000.00
Molecular weight molecular_weight201910.0 kDa
Excluded volume excluded_volume257030 ų
Envelope volume envelope_volume322150 ų
Hydration-shell volume shell_volume68324 ų
Envelope diameter envelope_diameter126.5
Shell Rg shell_rg45.72
Envelope Rg envelope_rg37.94
Shape Rg shape_rg38.26
Total Rg total_rg38.40
Total atoms total_atoms14230
Residues n_residues1670
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 dmax129.2
Rg (real space) rg_real38.45
Rg uncertainty (real space) rg_real_error1.20
I(0) (real space) i0_real5.4350e+08
I(0) uncertainty (real space) i0_real_error1.0420e+07
Rg (reciprocal space) rg_reciprocal38.51
I(0) (reciprocal space) i0_reciprocal543500000.0000
Solution quality estimate total_estimate0.7959
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary47.2
Skewness Skewness skewness0.322
Kurtosis Kurtosis kurtosis-0.303
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha100000000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.790; Stabil: 0.992; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)