7ppb

2.4 angstrom crystal structure of bone morphogenetic protein receptor type II (BMPRII) extracellular domain in complex with BMP10

Method: X-RAY DIFFRACTION Dmax: 76.6 Å Quality: GOOD

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

Bone morphogenetic protein 10

Homo sapiens

UniProt O95393

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 317–424 Not recorded Bone morphogenetic protein receptor type-2 × 2 (Q13873) 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

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.

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

View Construct and Data Evidence
UniProt name BMP10_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–108; UniProt 317–424

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 27–150 Not recorded Bone morphogenetic protein 10 × 2 (O95393) 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

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.

5 other PDB entries and 10 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 B; PDBConstruct 2–125; UniProt 27–150

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 7ppb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7ppb
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7ppb
Deposition date deposition_date2021-09-13
Structure title title2.4 angstrom crystal structure of bone morphogenetic protein receptor type II (BMPRII) extracellular domain in complex with BMP10
Keywords keywordsBMPRII BMP10 TGF-beta ligand and receptor Signalling complex, 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_guinier21.28
Radius of gyration Rg (electron density) rg_electron21.04
Forward intensity I(0) i09404940.00
Molecular weight molecular_weight22373.0 kDa
Excluded volume excluded_volume27805 ų
Envelope volume envelope_volume34363 ų
Hydration-shell volume shell_volume15208 ų
Envelope diameter envelope_diameter77.9
Shell Rg shell_rg25.41
Envelope Rg envelope_rg21.63
Shape Rg shape_rg21.01
Total Rg total_rg21.78
Total atoms total_atoms1564
Residues n_residues199
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 dmax76.6
Rg (real space) rg_real21.53
Rg uncertainty (real space) rg_real_error0.71
I(0) (real space) i0_real9.4050e+06
I(0) uncertainty (real space) i0_real_error1.3730e+05
Rg (reciprocal space) rg_reciprocal21.49
I(0) (reciprocal space) i0_reciprocal9405000.0000
Solution quality estimate total_estimate0.8043
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.3
Skewness Skewness skewness0.579
Kurtosis Kurtosis kurtosis-0.240
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1147000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.653; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.525; Smooth: 0.969

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)