5xpr

Human endothelin receptor type-B in complex with antagonist bosentan

Method: X-RAY DIFFRACTION Dmax: 97.0 Å Quality: REASONABLE

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

Endothelin B receptor,Endolysin,Endothelin B receptor

Homo sapiens

UniProt P00720

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 Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 61–161 Mutation:R124Y,K270A,C1054A,I1094R,S342A,I381A,C396A,C400A,C405A K86 4-tert-butyl-N-[6-(2-hydroxyethyloxy)-5-(2-methoxyphenoxy)-2-pyrimidin-2-yl-pyrimidin-4-yl]benzenesulfonamide × 1 SO4 SULFATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;pH 6;293 K;PEG 500 DME, Na2SO4, MOPS Resolution 3.60 Å R-free 0.297

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.

721 other PDB entries and 846 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ENLYS_BPT4
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 258–358; UniProt 61–161

Endothelin B receptor,Endolysin,Endothelin B receptor

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 Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 66–303 Chain A; UniProt 311–407 Mutation:R124Y,K270A,C1054A,I1094R,S342A,I381A,C396A,C400A,C405A K86 4-tert-butyl-N-[6-(2-hydroxyethyloxy)-5-(2-methoxyphenoxy)-2-pyrimidin-2-yl-pyrimidin-4-yl]benzenesulfonamide × 1 SO4 SULFATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;pH 6;293 K;PEG 500 DME, Na2SO4, MOPS Resolution 3.60 Å R-free 0.297

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 359–455; UniProt 311–407

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 5xpr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5xpr
Deposition date deposition_date2017-06-04
Structure title titleHuman endothelin receptor type-B in complex with antagonist bosentan
Keywords keywordsalpha helical, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.42
Radius of gyration Rg (electron density) rg_electron27.50
Forward intensity I(0) i031678400.00
Molecular weight molecular_weight45956.0 kDa
Excluded volume excluded_volume58537 ų
Envelope volume envelope_volume74719 ų
Hydration-shell volume shell_volume23978 ų
Envelope diameter envelope_diameter102.2
Shell Rg shell_rg33.11
Envelope Rg envelope_rg27.73
Shape Rg shape_rg27.48
Total Rg total_rg28.20
Total atoms total_atoms3229
Residues n_residues411
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 dmax97.0
Rg (real space) rg_real28.68
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real3.1680e+07
I(0) uncertainty (real space) i0_real_error4.3190e+05
Rg (reciprocal space) rg_reciprocal28.60
I(0) (reciprocal space) i0_reciprocal31680000.0000
Solution quality estimate total_estimate0.6317
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary24.2
Skewness Skewness skewness0.435
Kurtosis Kurtosis kurtosis-0.520
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha5392000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.762; Stabil: 1.000; Sysdev: 0.109; Positv: 1.000; Valcen: 0.651; Smooth: 0.944

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)