6igk

Crystal Structure of human ETB receptor in complex with Endothelin-3

Method: X-RAY DIFFRACTION Dmax: 101.1 Å Quality: GOOD

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

Endothelin receptor type B,Endolysin,Endothelin receptor type B

Homo sapiens

UniProt A0A097J809

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–161 Mutation:R124Y,D154A,K270A,C1052T,C1095A,S342A,I381A,C396A,C400A,C405A Endothelin-3 × 1 (P14138) OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 12 CIT CITRIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;pH 6;293 K;PEG 500DME, Ammonium citrate tribasic Resolution 2.00 Å R-free 0.227

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.

16 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A097J809_BPT4
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 242–401; UniProt 2–161

Endothelin receptor type B,Endolysin,Endothelin receptor type B

Homo sapiens

UniProt P24530

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 66–303 Chain A; UniProt 311–407 Mutation:R124Y,D154A,K270A,C1052T,C1095A,S342A,I381A,C396A,C400A,C405A Endothelin-3 × 1 (P14138) OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 12 CIT CITRIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;pH 6;293 K;PEG 500DME, Ammonium citrate tribasic Resolution 2.00 Å R-free 0.227

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 EDNRB_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–241; UniProt 66–303 Author chain A; PDBConstruct 402–498; UniProt 311–407

Endothelin-3

OrganismNot specified

UniProt P14138

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 97–117 Not recorded Endothelin receptor type B,Endolysin,Endothelin receptor type B × 1 (P24530,A0A097J809) OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 12 CIT CITRIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;pH 6;293 K;PEG 500DME, Ammonium citrate tribasic Resolution 2.00 Å R-free 0.227

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name EDN3_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–21; UniProt 97–117

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 6igk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6igk
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6igk
Deposition date deposition_date2018-09-25
Structure title titleCrystal Structure of human ETB receptor in complex with Endothelin-3
Keywords keywordsalpha helical, SIGNALING PROTEIN-PROTEIN BINDING complex; SIGNALING PROTEIN/PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.33
Radius of gyration Rg (electron density) rg_electron30.33
Forward intensity I(0) i045754100.00
Molecular weight molecular_weight59848.0 kDa
Excluded volume excluded_volume77915 ų
Envelope volume envelope_volume95475 ų
Hydration-shell volume shell_volume27982 ų
Envelope diameter envelope_diameter107.4
Shell Rg shell_rg35.24
Envelope Rg envelope_rg30.28
Shape Rg shape_rg30.33
Total Rg total_rg30.85
Total atoms total_atoms4207
Residues n_residues492
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 dmax101.1
Rg (real space) rg_real31.61
Rg uncertainty (real space) rg_real_error1.08
I(0) (real space) i0_real4.5750e+07
I(0) uncertainty (real space) i0_real_error7.5280e+05
Rg (reciprocal space) rg_reciprocal31.50
I(0) (reciprocal space) i0_reciprocal45750000.0000
Solution quality estimate total_estimate0.7698
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.8
Skewness Skewness skewness0.406
Kurtosis Kurtosis kurtosis-0.668
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10830000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.802; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.602; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)