5bkf

Cyro-EM structure of human Glycine Receptor alpha2-beta heteromer, Glycine bound, desensitized state

Method: ELECTRON MICROSCOPY Dmax: 123.3 Å Quality: REASONABLE

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

Glycine receptor subunit alpha-2

Homo sapiens

UniProt P23416

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 28–343 Chain A; UniProt 409–452 Chain B; UniProt 28–343 Chain B; UniProt 409–452 Chain C; UniProt 28–343 Chain C; UniProt 409–452 Chain D; UniProt 28–343 Chain D; UniProt 409–452 Mutation:second cytoplasmic domain deleted Glycine receptor subunit beta,Green fluorescent protein × 1 (P48167,P42212) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 GLY GLYCINE × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GLRA2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–316; UniProt 28–343 Author chain A; PDBConstruct 321–364; UniProt 409–452 Author chain B; PDBConstruct 1–316; UniProt 28–343 Author chain B; PDBConstruct 321–364; UniProt 409–452 Author chain C; PDBConstruct 1–316; UniProt 28–343 Author chain C; PDBConstruct 321–364; UniProt 409–452 Author chain D; PDBConstruct 1–316; UniProt 28–343 Author chain D; PDBConstruct 321–364; UniProt 409–452

Glycine receptor subunit beta,Green fluorescent protein

Homo sapiens

UniProt P42212

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 2–238 Mutation:four substitutions in the GFP portion Glycine receptor subunit alpha-2 × 4 (P23416) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 GLY GLYCINE × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 362–598; UniProt 2–238

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 Mutation:four substitutions in the GFP portion Glycine receptor subunit alpha-2 × 4 (P23416) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 GLY GLYCINE × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

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 23–353; UniProt 25–355 Author chain E; PDBConstruct 605–702; 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 5bkf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5bkf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5bkf
Deposition date deposition_date2021-03-19
Structure title titleCyro-EM structure of human Glycine Receptor alpha2-beta heteromer, Glycine bound, desensitized state
Keywords keywordsglycine receptor, alpha2-beta hetero-pentamer, glycine, MEMBRANE PROTEIN, SIGNALING PROTEIN; MEMBRANE PROTEIN, SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.94
Radius of gyration Rg (electron density) rg_electron37.45
Forward intensity I(0) i0490799000.00
Molecular weight molecular_weight191110.0 kDa
Excluded volume excluded_volume243100 ų
Envelope volume envelope_volume308100 ų
Hydration-shell volume shell_volume66855 ų
Envelope diameter envelope_diameter126.8
Shell Rg shell_rg44.99
Envelope Rg envelope_rg36.99
Shape Rg shape_rg37.50
Total Rg total_rg37.73
Total atoms total_atoms13470
Residues n_residues1689
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 dmax123.3
Rg (real space) rg_real37.84
Rg uncertainty (real space) rg_real_error0.71
I(0) (real space) i0_real4.9080e+08
I(0) uncertainty (real space) i0_real_error7.2820e+06
Rg (reciprocal space) rg_reciprocal37.91
I(0) (reciprocal space) i0_reciprocal490800000.0000
Solution quality estimate total_estimate0.6662
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.0
Skewness Skewness skewness0.318
Kurtosis Kurtosis kurtosis-0.294
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha86400000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.844; Stabil: 1.000; Sysdev: 0.080; Positv: 1.000; Valcen: 0.989; Smooth: 0.895

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)