SAXSdb — 7u5o

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

Inhibin beta B chain

Homo sapiens

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 293–407	Not recorded	Bone morphogenetic protein receptor type-2 × 1 （Q13873）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.4；294 K；175 mM Ammonium Sulfate 100 mM Bis Tris 14% PEG 3000	Resolution 3.45 Å R-free 0.284
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 293–407	Not recorded	Bone morphogenetic protein receptor type-2 × 1 （Q13873）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.4；294 K；175 mM Ammonium Sulfate 100 mM Bis Tris 14% PEG 3000	Resolution 3.45 Å R-free 0.284
3	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 293–407	Not recorded	Bone morphogenetic protein receptor type-2 × 1 （Q13873）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.4；294 K；175 mM Ammonium Sulfate 100 mM Bis Tris 14% PEG 3000	Resolution 3.45 Å R-free 0.284

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	INHBB_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–115； UniProt 293–407 Author chain B； PDBConstruct 1–115； UniProt 293–407 Author chain C； PDBConstruct 1–115； UniProt 293–407

Bone morphogenetic protein receptor type-2

Homo sapiens

UniProt Q13873

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 E； UniProt 27–137	Not recorded	Inhibin beta B chain × 1 （P09529）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.4；294 K；175 mM Ammonium Sulfate 100 mM Bis Tris 14% PEG 3000	Resolution 3.45 Å R-free 0.284
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain F； UniProt 27–137	Not recorded	Inhibin beta B chain × 1 （P09529）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.4；294 K；175 mM Ammonium Sulfate 100 mM Bis Tris 14% PEG 3000	Resolution 3.45 Å R-free 0.284
3	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain G； UniProt 27–137	Not recorded	Inhibin beta B chain × 1 （P09529）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.4；294 K；175 mM Ammonium Sulfate 100 mM Bis Tris 14% PEG 3000	Resolution 3.45 Å R-free 0.284

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 7U5O	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3G2F Crystal structure of the kinase domain of bone morphogenetic protein receptor type II (BMPR2) at 2.35 A resolution Deposited 2009-01-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 189–517（329 aa） Fragment：UNP residues 189-517, protein kinase domain	Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 SO4 SULFATE ION × 1 EDO 1,2-ETHANEDIOL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；277 K；0.3M ammonium_sulfate, 25% w/v PEG 8000, 0.1M Cacodylate pH6.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.35 Å R-free 0.246
3G2F Crystal structure of the kinase domain of bone morphogenetic protein receptor type II (BMPR2) at 2.35 A resolution Deposited 2009-01-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 189–517（329 aa） Fragment：UNP residues 189-517, protein kinase domain	Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 SO4 SULFATE ION × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；277 K；0.3M ammonium_sulfate, 25% w/v PEG 8000, 0.1M Cacodylate pH6.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.35 Å R-free 0.246
6UNP Crystal structure of the kinase domain of BMPR2-D485G Deposited 2019-10-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 188–529（342 aa） Fragment：kinase domain	Mutation：D485G Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 7 SO4 SULFATE ION × 3 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；277 K；0.1 M Na Cacodylate, pH 6.0, 0.3 M Ammonium sulfate, 22% w/v PEG 8000	Resolution 2.30 Å R-free 0.211
6UNP Crystal structure of the kinase domain of BMPR2-D485G Deposited 2019-10-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 188–529（342 aa） Fragment：kinase domain	Mutation：D485G Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 11 SO4 SULFATE ION × 2 EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；277 K；0.1 M Na Cacodylate, pH 6.0, 0.3 M Ammonium sulfate, 22% w/v PEG 8000	Resolution 2.30 Å R-free 0.211
7PPA High resolution structure of bone morphogenetic protein receptor type II (BMPRII) extracellular domain in complex with BMP10 Deposited 2021-09-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 27–150（124 aa） Chain D 27–150（124 aa）	Not recorded	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.8；294.15 K；14% PEG 3350 0.19 M Ammonium citrate dibasic 0.02 M Sodium citrate tribasic dihydrate	Resolution 1.48 Å R-free 0.207
7PPB 2.4 angstrom crystal structure of bone morphogenetic protein receptor type II (BMPRII) extracellular domain in complex with BMP10 Deposited 2021-09-13	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 27–150（124 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；294.15 K；14% PEG 3350 0.14 M KCl	Resolution 2.40 Å R-free 0.235
7PPC Ternary signalling complex of BMP10 bound to ALK1 and BMPRII Deposited 2021-09-13	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain I 27–150（124 aa） Chain J 27–150（124 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；294.15 K；20% PEG 3350 0.2 M Calcium acetate hydrate	Resolution 3.60 Å R-free 0.282
7PPC Ternary signalling complex of BMP10 bound to ALK1 and BMPRII Deposited 2021-09-13	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain K 27–150（124 aa） Chain L 27–150（124 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；294.15 K；20% PEG 3350 0.2 M Calcium acetate hydrate	Resolution 3.60 Å R-free 0.282

5 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	BMPR2_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain E； PDBConstruct 1–111； UniProt 27–137 Author chain F； PDBConstruct 1–111； UniProt 27–137 Author chain G； PDBConstruct 1–111； UniProt 27–137

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	7u5o
Deposition date deposition_date	2022-03-02
Structure title title	CRYSTAL STRUCTURE OF THE BONE MORPHOGENETIC PROTEIN RECEPTOR TYPE 2 LIGAND BINDING DOMAIN IN COMPLEX WITH ACTIVIN-B
Keywords keywords	Cell Signaling, Receptor-ligand complex, Growth factor, Receptor interaction, Activin B, BMPRII, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	32.34 Å
Radius of gyration Rg (electron density) rg_electron	31.45 Å
Forward intensity I(0) i0	71554400.00
Molecular weight molecular_weight	62547.0 kDa
Excluded volume excluded_volume	76412 Å³
Envelope volume envelope_volume	118440 Å³
Hydration-shell volume shell_volume	32329 Å³
Envelope diameter envelope_diameter	100.4 Å
Shell Rg shell_rg	37.52 Å
Envelope Rg envelope_rg	30.41 Å
Shape Rg shape_rg	31.46 Å
Total Rg total_rg	32.02 Å
Total atoms total_atoms	4357
Residues n_residues	587
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	94.3 Å
Rg (real space) rg_real	32.09 Å
Rg uncertainty (real space) rg_real_error	0.55 Å
I(0) (real space) i0_real	7.1550e+07
I(0) uncertainty (real space) i0_real_error	1.0360e+06
Rg (reciprocal space) rg_reciprocal	32.20 Å
I(0) (reciprocal space) i0_reciprocal	71560000.0000
Solution quality estimate total_estimate	0.9133
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	0
Primary peak position r_peak_primary	— Å
Skewness Skewness skewness	-0.072
Kurtosis Kurtosis kurtosis	-0.663
Angular range angular_range	— – 0.2450 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2947000.0000
Real-space data points n_real_points	50
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.979; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.937

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Inhibin beta B chain
Molecular weight formula_weight	12825.6 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	4357

GLECDGRTNLCCRQQFFIDFRLIGWNDWIIAPTGYYGNYCEGSCPAYLAGVPGSASSFHTAVVNQYRMRGLNPGTVNSCCIPTKLSTMSMLYFDDEYNIVKRDVPNMIVEECGCA

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Cricetulus griseus

Entity 2 Entity 2 polymer

Description description	Bone morphogenetic protein receptor type-2
Molecular weight formula_weight	12427.7 kDa
EC 编号 ec_number	2.7.11.30
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,F,G

SQNQERLCAFKDPYQQDLGIGESRISHENGTILCSKGSTCYGLWEKSKGDINLVKQGCWSHIGDPQECHYEECVVTTTPPSIQNGTYRFCCCSTDLCNVNFTENFPPPDTT

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Cricetulus griseus

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8. Citations (1)

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Unit-cell length a length_a	80.960 Å
Unit-cell length b length_b	115.460 Å
Unit-cell length c length_c	110.160 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	100.92 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	3.450 Å
Low-resolution limit resolution_low	36.060 Å
R factor r_factor	0.2381
R_work r_work	0.2357
R_free r_free	0.2844

fit	/app/data/saxs_computation/u5/7u5o/7u5o.fit
pddf	/app/data/pr_computation/u5/7u5o/7u5o.pr.out
profile	/app/data/saxs_computation/u5/7u5o/7u5o.dat

CRYSTAL STRUCTURE OF THE BONE MORPHOGENETIC PROTEIN RECEPTOR TYPE 2 LIGAND BINDING DOMAIN IN COMPLEX WITH ACTIVIN-B

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

Inhibin beta B chain

State in the Current Structure

Other States of the Same Protein in the Database

Bone morphogenetic protein receptor type-2

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

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)