SAXSdb — 1v6r

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

Endothelin-1

OrganismNot specified

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 53–73	Not recorded	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 3；297.7 K；Ionic strength (raw mmCIF value) 5% acetic acid；Pressure ambient NMR sample composition：2.5mM Endothelin-1 \| 90% H2O, 5% D2O, 5% deuterated acetic acid	Resolution not provided

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.

Other PDB	Difference from Current Entry 1V6R	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1EDN HUMAN ENDOTHELIN-1 Deposited 1994-09-19	Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 53–73（21 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.18 Å
1EDP CONFORMATIONAL ISOMERISM OF ENDOTHELIN IN ACIDIC AQUEOUS MEDIA: A QUANTITATIVE NOESY ANALYSIS Deposited 1991-12-16	Different construct Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 53–69（17 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1T7H X-ray structure of [Lys(-2)-Arg(-1)-des(17-21)]-endothelin-1 peptide Deposited 2004-05-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 51–68（18 aa） Chain B 51–68（18 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；291 K；PEG 4000, isopropanol, sodium citrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 291.0K, pH 5.00	Resolution 1.13 Å R-free 0.134
5GLH Human endothelin receptor type-B in complex with ET-1 Deposited 2016-07-11	Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 53–73（21 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions LIPIDIC CUBIC PHASE；pH 6；293 K；PEG 400, MES, (NH4)2SO4, 1,4-butanediol	Resolution 2.80 Å R-free 0.277
6DK5 The X-ray crystal structure of human endothelin-1, a polypeptide hormone regulator of blood pressure Deposited 2018-05-28	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 53–73（21 aa） Fragment：UNP residues 53-73	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；310 K；4 uL 15 mg/mL aqueous endothelin + 6 uL reservoir solution (20-25% MPD, 0.2 M MES, pH 6.5) + 2 uL 0.2 M MES, pH 6.5	Resolution 1.85 Å R-free 0.284
6DK5 The X-ray crystal structure of human endothelin-1, a polypeptide hormone regulator of blood pressure Deposited 2018-05-28	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 53–73（21 aa） Fragment：UNP residues 53-73	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；310 K；4 uL 15 mg/mL aqueous endothelin + 6 uL reservoir solution (20-25% MPD, 0.2 M MES, pH 6.5) + 2 uL 0.2 M MES, pH 6.5	Resolution 1.85 Å R-free 0.284
8HCQ Cryo-EM structure of endothelin1-bound ETAR-Gq complex Deposited 2022-11-02	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric	Chain L 53–73（21 aa） Fragment：UNP residues 53-73	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.01 Å
8HCX Cryo-EM structure of Endothelin1-bound ETBR-Gq complex Deposited 2022-11-03	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric	Chain D 53–73（21 aa） Fragment：UNP residues 53-73	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
8IY5 ETB-Gi complex bound to endothelin-1 Deposited 2023-04-04	Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain L 53–73（21 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
8IY6 ETB-Gi complex bound to Endotheline-1, focused on receptor Deposited 2023-04-04	Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain L 53–73（21 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.13 Å
8XGR ETB-eGt complex bound to endothelin-1 Deposited 2023-12-15	Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain L 53–73（21 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8XVH Cryo-EM structure of ETBR bound with Endothelin1 Deposited 2024-01-15	Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric	Chain T 53–73（21 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.26 Å
8XVI Cryo-EM structure of ETAR bound with Endothelin1 Deposited 2024-01-15	Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric	Chain T 53–73（21 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.32 Å
8XWP Cryo-EM structure of ET-1 bound ETBR-DNGI complex Deposited 2024-01-16	Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain L 53–73（21 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.21 Å
8XWQ Cryo-EM structure of ET-1 bound ETBR-DNGI complex Deposited 2024-01-16	Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain L 53–73（21 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.60 Å
8ZRT Cryo-EM structure focused on the receptor of the ET-1 bound ETBR-DNGI complex Deposited 2024-06-05	Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain L 53–73（21 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.62 Å

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	1
Chains and sequence ranges	Author chain A； 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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1v6r
Deposition date deposition_date	2003-12-03
Structure title title	Solution Structure of Endothelin-1 with its C-terminal Folding
Keywords keywords	endothelin, a-helix, c-terminal folding, cardiovascular bioactive peptide, g-protein coupled-receptor ligand, CONTRACTILE PROTEIN; CONTRACTILE PROTEIN
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	7.31 Å
Radius of gyration Rg (electron density) rg_electron	7.81 Å
Forward intensity I(0) i0	37474000.00
Molecular weight molecular_weight	49879.0 kDa
Excluded volume excluded_volume	61544 Å³
Envelope volume envelope_volume	4440 Å³
Hydration-shell volume shell_volume	4926 Å³
Envelope diameter envelope_diameter	27.9 Å
Shell Rg shell_rg	12.98 Å
Envelope Rg envelope_rg	8.80 Å
Shape Rg shape_rg	7.77 Å
Total Rg total_rg	8.12 Å
Total atoms total_atoms	6560
Residues n_residues	420
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	25.7 Å
Rg (real space) rg_real	7.30 Å
Rg uncertainty (real space) rg_real_error	0.31 Å
I(0) (real space) i0_real	3.7470e+07
I(0) uncertainty (real space) i0_real_error	3.9120e+05
Rg (reciprocal space) rg_reciprocal	7.30 Å
I(0) (reciprocal space) i0_reciprocal	37470000.0000
Solution quality estimate total_estimate	0.8713
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	9.1 Å
Skewness Skewness skewness	0.100
Kurtosis Kurtosis kurtosis	-0.818
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2348.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.849; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.871; Smooth: 0.909

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1v6ra_
Class class	j — Peptides
Fold Fold fold	j.28 — Endothelin-like
Superfamily Superfamily superfamily	j.28.1 — Endothelin-like
Family Family family	j.28.1.1 — Endothelin-like

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8. Citations (1)

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Description description	Endothelin-1
Molecular weight formula_weight	2498.0 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	6560

fit	/app/data/saxs_computation/v6/1v6r/1v6r.fit
pddf	/app/data/pr_computation/v6/1v6r/1v6r.pr.out
profile	/app/data/saxs_computation/v6/1v6r/1v6r.dat

Solution Structure of Endothelin-1 with its C-terminal Folding

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

Endothelin-1

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)