9boz

Cryo-EM structure of human Glycine Receptor alpha3-beta heteromer in presence of glycine

Method: ELECTRON MICROSCOPY Dmax: 124.2 Å Quality: GOOD

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

Glycine receptor subunit alpha-3

Homo sapiens

UniProt O75311

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 34–464 Chain B; UniProt 34–464 Chain C; UniProt 34–464 Chain D; UniProt 34–464 Not recorded Glycine receptor subunit beta,Green fluorescent protein × 1 (P48167,A0A9X4KGN5) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.84 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.

18 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GLRA3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–422; UniProt 34–464 Author chain B; PDBConstruct 1–422; UniProt 34–464 Author chain C; PDBConstruct 1–422; UniProt 34–464 Author chain D; PDBConstruct 1–422; UniProt 34–464

Glycine receptor subunit beta,Green fluorescent protein

Homo sapiens

UniProt A0A9X4KGN5

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 9–248 Not recorded Glycine receptor subunit alpha-3 × 4 (O75311) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.84 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A9X4KGN5_9BACI
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 339–578; UniProt 9–248

Glycine receptor subunit beta,Green fluorescent protein

Homo sapiens

UniProt P48167

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 25–355 Chain E; UniProt 400–497 Not recorded Glycine receptor subunit alpha-3 × 4 (O75311) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.84 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.

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GLRB_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–331; UniProt 25–355 Author chain E; PDBConstruct 583–680; UniProt 400–497

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 9boz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9boz
Deposition date deposition_date2024-05-06
Structure title titleCryo-EM structure of human Glycine Receptor alpha3-beta heteromer in presence of glycine
Keywords keywordsglycine receptor subunit alpha-3, glycine receptor subunit beta, Green fluorescent protein, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier38.93
Radius of gyration Rg (electron density) rg_electron38.49
Forward intensity I(0) i0505773000.00
Molecular weight molecular_weight194650.0 kDa
Excluded volume excluded_volume247800 ų
Envelope volume envelope_volume322530 ų
Hydration-shell volume shell_volume68413 ų
Envelope diameter envelope_diameter133.1
Shell Rg shell_rg45.72
Envelope Rg envelope_rg38.03
Shape Rg shape_rg38.52
Total Rg total_rg38.78
Total atoms total_atoms13723
Residues n_residues1705
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 dmax124.2
Rg (real space) rg_real38.84
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real5.0580e+08
I(0) uncertainty (real space) i0_real_error9.2470e+06
Rg (reciprocal space) rg_reciprocal38.90
I(0) (reciprocal space) i0_reciprocal505800000.0000
Solution quality estimate total_estimate0.8702
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.5
Skewness Skewness skewness0.332
Kurtosis Kurtosis kurtosis-0.283
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha90520000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.872; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.703

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)