SAXSdb — 2k1v

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

Relaxin-3

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 26–52	Fragment：Relaxin-3 B chain	Insulin-like peptide INSL5 × 1 （Q9Y5Q6）	SOLUTION NMR NMR measurement conditions：pH 4；298 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR sample composition：1 mM relaxin-3 B-chain, 1 mM INSL5 A-chain, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition：1 mM relaxin-3 B-chain, 1 mM INSL5 A-chain, 100% D2O \| 100% D2O	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 2K1V	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2FHW Solution structure of human relaxin-3 Deposited 2005-12-27	Different construct Different mutation/modification Different oligomeric state Different experimental conditions	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 119–142（24 aa） Fragment：Relaxin 3 A chain Chain B 26–52（27 aa） Fragment：Relaxin 3 B chain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3；298 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR measurement conditions pH 3；303 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR measurement conditions pH 3；293 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR sample composition 1mM human relaxin-3; 90% H2O, 10% D2O \| 90% H2O/10% D2O NMR sample composition 1mM human relaxin-3; 100% D2O \| 100% D2O	Resolution not provided
9KFI Cryo-EM structure of the human relaxin family peptide receptor 3 in complex with relaxin-3 and G protein Deposited 2024-11-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 7 PDB declaration: heptameric	Chain A 119–142（24 aa） Chain B 31–52（22 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.91 Å
9KFK Cryo-EM structure of the relaxin-3-bound human relaxin family peptide receptor 4 (RXFP4)-Gi complex Deposited 2024-11-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 7 PDB declaration: heptameric	Chain A 119–142（24 aa） Chain B 34–52（19 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.95 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	REL3_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain B； PDBConstruct 1–27； UniProt 26–52

Insulin-like peptide INSL5

OrganismNot specified

UniProt Q9Y5Q6

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 116–135	Fragment：Insulin-like peptide INSL5 A chain Non-standard monomer：Yes (specific site not provided by mmCIF)	Relaxin-3 × 1 （Q8WXF3）	SOLUTION NMR NMR measurement conditions：pH 4；298 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR sample composition：1 mM relaxin-3 B-chain, 1 mM INSL5 A-chain, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition：1 mM relaxin-3 B-chain, 1 mM INSL5 A-chain, 100% D2O \| 100% D2O	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 2K1V	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
7YJ4 Cryo-EM structure of the INSL5-bound human relaxin family peptidereceptor 4 (RXFP4)-Gi complex Deposited 2022-07-19	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain A 115–135（21 aa） Chain B 23–46（24 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.19 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	INSL5_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain A； PDBConstruct 2–21； UniProt 116–135

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	2k1v
Deposition date deposition_date	2008-03-17
Structure title title	R3/I5 relaxin chimera
Keywords keywords	peptide hormone, relaxin-3, insl5, chimera, Cleavage on pair of basic residues, Secreted, SIGNALING PROTEIN, HORMONE; HORMONE
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	9.96 Å
Radius of gyration Rg (electron density) rg_electron	9.96 Å
Forward intensity I(0) i0	180005000.00
Molecular weight molecular_weight	104940.0 kDa
Excluded volume excluded_volume	128160 Å³
Envelope volume envelope_volume	10790 Å³
Hydration-shell volume shell_volume	8344 Å³
Envelope diameter envelope_diameter	38.2 Å
Shell Rg shell_rg	16.72 Å
Envelope Rg envelope_rg	11.85 Å
Shape Rg shape_rg	9.98 Å
Total Rg total_rg	10.10 Å
Total atoms total_atoms	14260
Residues n_residues	940
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	34.3 Å
Rg (real space) rg_real	9.96 Å
Rg uncertainty (real space) rg_real_error	0.32 Å
I(0) (real space) i0_real	1.8000e+08
I(0) uncertainty (real space) i0_real_error	1.9610e+06
Rg (reciprocal space) rg_reciprocal	9.96 Å
I(0) (reciprocal space) i0_reciprocal	180000000.0000
Solution quality estimate total_estimate	0.8846
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	12.6 Å
Skewness Skewness skewness	0.237
Kurtosis Kurtosis kurtosis	-0.391
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	18430.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.875; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.914; Smooth: 0.955

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Description description	Relaxin-3
Molecular weight formula_weight	3047.6 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	B
Atom count atom_count	14260

Description description	Insulin-like peptide INSL5
Molecular weight formula_weight	2202.5 kDa
Source method src_method	syn
Copy count entity_count	1

R3/I5 relaxin chimera

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

Relaxin-3

State in the Current Structure

Other States of the Same Protein in the Database

Insulin-like peptide INSL5

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

Unit cell Unit Cell

Symmetry Symmetry

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/k1/2k1v/2k1v.fit
pddf	/app/data/pr_computation/k1/2k1v/2k1v.pr.out
profile	/app/data/saxs_computation/k1/2k1v/2k1v.dat