8xgr

ETB-eGt complex bound to endothelin-1

Method: ELECTRON MICROSCOPY Dmax: 120.5 Å Quality: GOOD

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

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2,eGt-alpha

Bos taurus

UniProt P63212

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain G; UniProt 1–71 Not recorded Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 Camelid antibody VHH fragment × 1 Endothelin receptor type B × 1 Endothelin-1 × 1 (P05305) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

215 other PDB entries and 216 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBG2_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain G; PDBConstruct 1–71; UniProt 1–71

Endothelin-1

OrganismNot specified

UniProt P05305

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain L; UniProt 53–73 Not recorded Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2,eGt-alpha × 1 (P63212) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 Camelid antibody VHH fragment × 1 Endothelin receptor type B × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

15 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EDN1_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain L; PDBConstruct 1–21; UniProt 53–73

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 8xgr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8xgr
Deposition date deposition_date2023-12-15
Structure title titleETB-eGt complex bound to endothelin-1
Keywords keywordsSIGNALING PROTEIN, PEPTIDE BINDING PROTEIN-IMMUNE SYSTEM complex; PEPTIDE BINDING PROTEIN/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.47
Radius of gyration Rg (electron density) rg_electron36.53
Forward intensity I(0) i0206359000.00
Molecular weight molecular_weight117020.0 kDa
Excluded volume excluded_volume146980 ų
Envelope volume envelope_volume192010 ų
Hydration-shell volume shell_volume45110 ų
Envelope diameter envelope_diameter128.8
Shell Rg shell_rg41.41
Envelope Rg envelope_rg36.36
Shape Rg shape_rg36.51
Total Rg total_rg36.93
Total atoms total_atoms8206
Residues n_residues1049
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 dmax120.5
Rg (real space) rg_real36.68
Rg uncertainty (real space) rg_real_error0.92
I(0) (real space) i0_real2.0640e+08
I(0) uncertainty (real space) i0_real_error3.4890e+06
Rg (reciprocal space) rg_reciprocal36.55
I(0) (reciprocal space) i0_reciprocal206300000.0000
Solution quality estimate total_estimate0.8584
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary36.4
Skewness Skewness skewness0.488
Kurtosis Kurtosis kurtosis-0.305
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha42120000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.863; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.903; Smooth: 0.662

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)