7ppc

Ternary signalling complex of BMP10 bound to ALK1 and BMPRII

Method: X-RAY DIFFRACTION D_max: 104.6 Å Quality: GOOD

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

Bone morphogenetic protein 10

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 × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain A； UniProt 317–424 Chain B； UniProt 317–424	Not recorded	Serine/threonine-protein kinase receptor R3 × 2 （P37023） Bone morphogenetic protein receptor type-2 × 2 （Q13873）	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
2	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain C； UniProt 317–424 Chain D； UniProt 317–424	Not recorded	Serine/threonine-protein kinase receptor R3 × 2 （P37023） Bone morphogenetic protein receptor type-2 × 2 （Q13873）	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

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 7PPC	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6SF1 Bone morphogenetic protein 10 (BMP10) complexed with extracellular domain of activin receptor-like kinase 1 (ALK1). Deposited 2019-07-30	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 B 317–424（108 aa）	Not recorded	NI NICKEL (II) ION × 10	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；17% PEG 3350, 0.175 M NH4I, 0.1 M HEPES pH 7.8	Resolution 2.80 Å R-free 0.279
6SF3 Bone morphogenetic protein 10 (BMP10) in complex with extracellular domain of activin receptor-like kinase 1 (ALK1) at 2.3 Angstrom Deposited 2019-07-31	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 317–424（108 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；0.07 M Amino acids (0.014 M DL-Glutamic acids monohydrate; 0.014 M DL-Alanine; 0.014 M Glycine; 0.014 M DL-Lysine monohydrochloride; 0.014 M DL-Serine), 0.07 M Buffer System 3 (0.07 M Tris(base)/BICINE), 35% Precipitant Mix 4 (9% v/v MPD, 9% w/v PEG 1000, 9% w/ PEG3350)	Resolution 2.30 Å R-free 0.243
7POI Prodomain bound BMP10 crystal form 1 Deposited 2021-09-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 317–424（108 aa） Chain B 317–424（108 aa） Chain C 22–316（295 aa） Chain D 22–316（295 aa）	Not recorded	TAR D(-)-TARTARIC ACID × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.6；294.15 K；19% PEG 3350 0.15 M Ammonium tartrate dibasic 0.02 M Sodium cacodylate trihydrate	Resolution 2.90 Å R-free 0.268
7POJ Prodomain bound BMP10 crystal form 2 Deposited 2021-09-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 317–424（108 aa） Chain B 317–424（108 aa） Chain C 22–316（295 aa） Chain D 22–316（295 aa）	Not recorded	PG4 TETRAETHYLENE GLYCOL × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.6；294.15 K；20% PEG3350 0.2 M ammonium tartrate dibasic	Resolution 3.50 Å R-free 0.300
7PPA High resolution structure of bone morphogenetic protein receptor type II (BMPRII) extracellular domain in complex with BMP10 Deposited 2021-09-13	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 317–424（108 aa） Chain B 317–424（108 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 mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 317–424（108 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
9DPY BMP-10 with BMP-9 Crystal Contacts Deposited 2024-09-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 320–424（105 aa） Chain B 320–424（105 aa）	Mutation：N357F, Y358F, A374T, Y409L, F411Y Mutation：N357F, Y358F, A374T, Y409L, F411Y	PO4 PHOSPHATE ION × 13 NA SODIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.2；293 K；25% (v/v) 1,2-propanediol, 100 mM sodium phosphate dibasic/potassium phosphate monobasic pH 6.2, 10% (v/v) glycerol	Resolution 1.77 Å R-free 0.251

7 other PDB entries and 7 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 Author chain B； PDBConstruct 1–108； UniProt 317–424 Author chain C； PDBConstruct 1–108； UniProt 317–424 Author chain D； PDBConstruct 1–108； UniProt 317–424

Serine/threonine-protein kinase receptor R3

Homo sapiens

UniProt P37023

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 × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain E； UniProt 22–118 Chain F； UniProt 22–118	Not recorded	Bone morphogenetic protein 10 × 2 （O95393） Bone morphogenetic protein receptor type-2 × 2 （Q13873）	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
2	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain G； UniProt 22–118 Chain H； UniProt 22–118	Not recorded	Bone morphogenetic protein 10 × 2 （O95393） Bone morphogenetic protein receptor type-2 × 2 （Q13873）	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

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 7PPC	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2LCR NMR Structure of Alk1 extracellular domain Deposited 2011-05-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 22–118（97 aa） Fragment：Extracellular domain residues 22-118	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；305 K；Pressure ambient NMR sample composition 0.5 mM [U-100% 15N] Alk1, 25 mM sodium phosphate, 0.02 % sodium azide, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N] Alk1, 25 mM sodium phosphate, 0.02 % sodium azide, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N] Alk1, 25 mM sodium phosphate, 0.02 % sodium azide, 5mg/mL mg Pf1 phage, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
3MY0 Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189 Deposited 2010-05-08	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 195–497（303 aa） Fragment：kinase domain (UNP residue 195-497)	Not recorded	LDN 4-[6-(4-piperazin-1-ylphenyl)pyrazolo[1,5-a]pyrimidin-3-yl]quinoline × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；16% PEG 3350, 0.2M Na/K PO4, 5% ethylene glycol, 2% glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K	Resolution 2.65 Å R-free 0.247
3MY0 Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189 Deposited 2010-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 10 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain J 195–497（303 aa） Fragment：kinase domain (UNP residue 195-497)	Not recorded	LDN 4-[6-(4-piperazin-1-ylphenyl)pyrazolo[1,5-a]pyrimidin-3-yl]quinoline × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；16% PEG 3350, 0.2M Na/K PO4, 5% ethylene glycol, 2% glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K	Resolution 2.65 Å R-free 0.247
3MY0 Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189 Deposited 2010-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 11 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain K 195–497（303 aa） Fragment：kinase domain (UNP residue 195-497)	Not recorded	LDN 4-[6-(4-piperazin-1-ylphenyl)pyrazolo[1,5-a]pyrimidin-3-yl]quinoline × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；16% PEG 3350, 0.2M Na/K PO4, 5% ethylene glycol, 2% glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K	Resolution 2.65 Å R-free 0.247
3MY0 Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189 Deposited 2010-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 12 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain L 195–497（303 aa） Fragment：kinase domain (UNP residue 195-497)	Not recorded	LDN 4-[6-(4-piperazin-1-ylphenyl)pyrazolo[1,5-a]pyrimidin-3-yl]quinoline × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；16% PEG 3350, 0.2M Na/K PO4, 5% ethylene glycol, 2% glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K	Resolution 2.65 Å R-free 0.247
3MY0 Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189 Deposited 2010-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 13 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain M 195–497（303 aa） Fragment：kinase domain (UNP residue 195-497)	Not recorded	LDN 4-[6-(4-piperazin-1-ylphenyl)pyrazolo[1,5-a]pyrimidin-3-yl]quinoline × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；16% PEG 3350, 0.2M Na/K PO4, 5% ethylene glycol, 2% glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K	Resolution 2.65 Å R-free 0.247
3MY0 Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189 Deposited 2010-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 14 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain N 195–497（303 aa） Fragment：kinase domain (UNP residue 195-497)	Not recorded	LDN 4-[6-(4-piperazin-1-ylphenyl)pyrazolo[1,5-a]pyrimidin-3-yl]quinoline × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；16% PEG 3350, 0.2M Na/K PO4, 5% ethylene glycol, 2% glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K	Resolution 2.65 Å R-free 0.247
3MY0 Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189 Deposited 2010-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 15 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain O 195–497（303 aa） Fragment：kinase domain (UNP residue 195-497)	Not recorded	LDN 4-[6-(4-piperazin-1-ylphenyl)pyrazolo[1,5-a]pyrimidin-3-yl]quinoline × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；16% PEG 3350, 0.2M Na/K PO4, 5% ethylene glycol, 2% glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K	Resolution 2.65 Å R-free 0.247
3MY0 Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189 Deposited 2010-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 16 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain P 195–497（303 aa） Fragment：kinase domain (UNP residue 195-497)	Not recorded	LDN 4-[6-(4-piperazin-1-ylphenyl)pyrazolo[1,5-a]pyrimidin-3-yl]quinoline × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；16% PEG 3350, 0.2M Na/K PO4, 5% ethylene glycol, 2% glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K	Resolution 2.65 Å R-free 0.247
3MY0 Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189 Deposited 2010-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 17 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain Q 195–497（303 aa） Fragment：kinase domain (UNP residue 195-497)	Not recorded	LDN 4-[6-(4-piperazin-1-ylphenyl)pyrazolo[1,5-a]pyrimidin-3-yl]quinoline × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；16% PEG 3350, 0.2M Na/K PO4, 5% ethylene glycol, 2% glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K	Resolution 2.65 Å R-free 0.247
3MY0 Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189 Deposited 2010-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 18 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain R 195–497（303 aa） Fragment：kinase domain (UNP residue 195-497)	Not recorded	LDN 4-[6-(4-piperazin-1-ylphenyl)pyrazolo[1,5-a]pyrimidin-3-yl]quinoline × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；16% PEG 3350, 0.2M Na/K PO4, 5% ethylene glycol, 2% glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K	Resolution 2.65 Å R-free 0.247
3MY0 Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189 Deposited 2010-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 19 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain S 195–497（303 aa） Fragment：kinase domain (UNP residue 195-497)	Not recorded	LDN 4-[6-(4-piperazin-1-ylphenyl)pyrazolo[1,5-a]pyrimidin-3-yl]quinoline × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；16% PEG 3350, 0.2M Na/K PO4, 5% ethylene glycol, 2% glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K	Resolution 2.65 Å R-free 0.247
3MY0 Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189 Deposited 2010-05-08	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 195–497（303 aa） Fragment：kinase domain (UNP residue 195-497)	Not recorded	LDN 4-[6-(4-piperazin-1-ylphenyl)pyrazolo[1,5-a]pyrimidin-3-yl]quinoline × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；16% PEG 3350, 0.2M Na/K PO4, 5% ethylene glycol, 2% glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K	Resolution 2.65 Å R-free 0.247
3MY0 Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189 Deposited 2010-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 20 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain T 195–497（303 aa） Fragment：kinase domain (UNP residue 195-497)	Not recorded	LDN 4-[6-(4-piperazin-1-ylphenyl)pyrazolo[1,5-a]pyrimidin-3-yl]quinoline × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；16% PEG 3350, 0.2M Na/K PO4, 5% ethylene glycol, 2% glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K	Resolution 2.65 Å R-free 0.247
3MY0 Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189 Deposited 2010-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 21 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain U 195–497（303 aa） Fragment：kinase domain (UNP residue 195-497)	Not recorded	LDN 4-[6-(4-piperazin-1-ylphenyl)pyrazolo[1,5-a]pyrimidin-3-yl]quinoline × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；16% PEG 3350, 0.2M Na/K PO4, 5% ethylene glycol, 2% glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K	Resolution 2.65 Å R-free 0.247
3MY0 Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189 Deposited 2010-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 22 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain V 195–497（303 aa） Fragment：kinase domain (UNP residue 195-497)	Not recorded	LDN 4-[6-(4-piperazin-1-ylphenyl)pyrazolo[1,5-a]pyrimidin-3-yl]quinoline × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；16% PEG 3350, 0.2M Na/K PO4, 5% ethylene glycol, 2% glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K	Resolution 2.65 Å R-free 0.247
3MY0 Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189 Deposited 2010-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 23 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain W 195–497（303 aa） Fragment：kinase domain (UNP residue 195-497)	Not recorded	LDN 4-[6-(4-piperazin-1-ylphenyl)pyrazolo[1,5-a]pyrimidin-3-yl]quinoline × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；16% PEG 3350, 0.2M Na/K PO4, 5% ethylene glycol, 2% glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K	Resolution 2.65 Å R-free 0.247
3MY0 Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189 Deposited 2010-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 24 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain X 195–497（303 aa） Fragment：kinase domain (UNP residue 195-497)	Not recorded	LDN 4-[6-(4-piperazin-1-ylphenyl)pyrazolo[1,5-a]pyrimidin-3-yl]quinoline × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；16% PEG 3350, 0.2M Na/K PO4, 5% ethylene glycol, 2% glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K	Resolution 2.65 Å R-free 0.247
3MY0 Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189 Deposited 2010-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 195–497（303 aa） Fragment：kinase domain (UNP residue 195-497)	Not recorded	LDN 4-[6-(4-piperazin-1-ylphenyl)pyrazolo[1,5-a]pyrimidin-3-yl]quinoline × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；16% PEG 3350, 0.2M Na/K PO4, 5% ethylene glycol, 2% glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K	Resolution 2.65 Å R-free 0.247
3MY0 Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189 Deposited 2010-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 195–497（303 aa） Fragment：kinase domain (UNP residue 195-497)	Not recorded	LDN 4-[6-(4-piperazin-1-ylphenyl)pyrazolo[1,5-a]pyrimidin-3-yl]quinoline × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；16% PEG 3350, 0.2M Na/K PO4, 5% ethylene glycol, 2% glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K	Resolution 2.65 Å R-free 0.247
3MY0 Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189 Deposited 2010-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain E 195–497（303 aa） Fragment：kinase domain (UNP residue 195-497)	Not recorded	LDN 4-[6-(4-piperazin-1-ylphenyl)pyrazolo[1,5-a]pyrimidin-3-yl]quinoline × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；16% PEG 3350, 0.2M Na/K PO4, 5% ethylene glycol, 2% glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K	Resolution 2.65 Å R-free 0.247
3MY0 Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189 Deposited 2010-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain F 195–497（303 aa） Fragment：kinase domain (UNP residue 195-497)	Not recorded	LDN 4-[6-(4-piperazin-1-ylphenyl)pyrazolo[1,5-a]pyrimidin-3-yl]quinoline × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；16% PEG 3350, 0.2M Na/K PO4, 5% ethylene glycol, 2% glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K	Resolution 2.65 Å R-free 0.247
3MY0 Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189 Deposited 2010-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 7 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain G 195–497（303 aa） Fragment：kinase domain (UNP residue 195-497)	Not recorded	LDN 4-[6-(4-piperazin-1-ylphenyl)pyrazolo[1,5-a]pyrimidin-3-yl]quinoline × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；16% PEG 3350, 0.2M Na/K PO4, 5% ethylene glycol, 2% glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K	Resolution 2.65 Å R-free 0.247
3MY0 Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189 Deposited 2010-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 8 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain H 195–497（303 aa） Fragment：kinase domain (UNP residue 195-497)	Not recorded	LDN 4-[6-(4-piperazin-1-ylphenyl)pyrazolo[1,5-a]pyrimidin-3-yl]quinoline × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；16% PEG 3350, 0.2M Na/K PO4, 5% ethylene glycol, 2% glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K	Resolution 2.65 Å R-free 0.247
3MY0 Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189 Deposited 2010-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 9 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain I 195–497（303 aa） Fragment：kinase domain (UNP residue 195-497)	Not recorded	LDN 4-[6-(4-piperazin-1-ylphenyl)pyrazolo[1,5-a]pyrimidin-3-yl]quinoline × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；16% PEG 3350, 0.2M Na/K PO4, 5% ethylene glycol, 2% glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K	Resolution 2.65 Å R-free 0.247
4FAO Specificity and Structure of a high affinity Activin-like 1 (ALK1) signaling complex Deposited 2012-05-22	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain C 22–118（97 aa） Fragment：Extracellular domain Chain D 22–118（97 aa） Fragment：Extracellular domain	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；293 K；20% PEG 3350, 0.2 M sodium malonate, 0.1 M Bis-Tris propane, pH 6.5, vapor diffusion, temperature 293K	Resolution 3.36 Å R-free 0.261
4FAO Specificity and Structure of a high affinity Activin-like 1 (ALK1) signaling complex Deposited 2012-05-22	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain I 22–118（97 aa） Fragment：Extracellular domain Chain J 22–118（97 aa） Fragment：Extracellular domain	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；293 K；20% PEG 3350, 0.2 M sodium malonate, 0.1 M Bis-Tris propane, pH 6.5, vapor diffusion, temperature 293K	Resolution 3.36 Å R-free 0.261
4FAO Specificity and Structure of a high affinity Activin-like 1 (ALK1) signaling complex Deposited 2012-05-22	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain O 22–118（97 aa） Fragment：Extracellular domain Chain P 22–118（97 aa） Fragment：Extracellular domain	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；293 K；20% PEG 3350, 0.2 M sodium malonate, 0.1 M Bis-Tris propane, pH 6.5, vapor diffusion, temperature 293K	Resolution 3.36 Å R-free 0.261
4FAO Specificity and Structure of a high affinity Activin-like 1 (ALK1) signaling complex Deposited 2012-05-22	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain U 22–118（97 aa） Fragment：Extracellular domain Chain V 22–118（97 aa） Fragment：Extracellular domain	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；293 K；20% PEG 3350, 0.2 M sodium malonate, 0.1 M Bis-Tris propane, pH 6.5, vapor diffusion, temperature 293K	Resolution 3.36 Å R-free 0.261
4FAO Specificity and Structure of a high affinity Activin-like 1 (ALK1) signaling complex Deposited 2012-05-22	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain c 22–118（97 aa） Fragment：Extracellular domain Chain d 22–118（97 aa） Fragment：Extracellular domain	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；293 K；20% PEG 3350, 0.2 M sodium malonate, 0.1 M Bis-Tris propane, pH 6.5, vapor diffusion, temperature 293K	Resolution 3.36 Å R-free 0.261
4FAO Specificity and Structure of a high affinity Activin-like 1 (ALK1) signaling complex Deposited 2012-05-22	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain i 22–118（97 aa） Fragment：Extracellular domain Chain j 22–118（97 aa） Fragment：Extracellular domain	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；293 K；20% PEG 3350, 0.2 M sodium malonate, 0.1 M Bis-Tris propane, pH 6.5, vapor diffusion, temperature 293K	Resolution 3.36 Å R-free 0.261
6SF1 Bone morphogenetic protein 10 (BMP10) complexed with extracellular domain of activin receptor-like kinase 1 (ALK1). Deposited 2019-07-30	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 A 21–118（98 aa）	Not recorded	NI NICKEL (II) ION × 10	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；17% PEG 3350, 0.175 M NH4I, 0.1 M HEPES pH 7.8	Resolution 2.80 Å R-free 0.279
6SF2 Ternary complex of human bone morphogenetic protein 9 (BMP9) growth factor domain, its prodomain and extracellular domain of activin receptor-like kinase 1 (ALK1). Deposited 2019-07-31	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 21–118（98 aa） Chain D 21–118（98 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；0.14 M potassium sodium tartrate, 14% PEG 3350	Resolution 3.30 Å R-free 0.274
6SF3 Bone morphogenetic protein 10 (BMP10) in complex with extracellular domain of activin receptor-like kinase 1 (ALK1) at 2.3 Angstrom Deposited 2019-07-31	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 21–118（98 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；0.07 M Amino acids (0.014 M DL-Glutamic acids monohydrate; 0.014 M DL-Alanine; 0.014 M Glycine; 0.014 M DL-Lysine monohydrochloride; 0.014 M DL-Serine), 0.07 M Buffer System 3 (0.07 M Tris(base)/BICINE), 35% Precipitant Mix 4 (9% v/v MPD, 9% w/v PEG 1000, 9% w/ PEG3350)	Resolution 2.30 Å R-free 0.243

6 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ACVL1_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain E； PDBConstruct 1–97； UniProt 22–118 Author chain F； PDBConstruct 1–97； UniProt 22–118 Author chain G； PDBConstruct 1–97； UniProt 22–118 Author chain H； PDBConstruct 1–97； UniProt 22–118

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 × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain I； UniProt 27–150 Chain J； UniProt 27–150	Not recorded	Bone morphogenetic protein 10 × 2 （O95393） Serine/threonine-protein kinase receptor R3 × 2 （P37023）	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
2	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain K； UniProt 27–150 Chain L； UniProt 27–150	Not recorded	Bone morphogenetic protein 10 × 2 （O95393） Serine/threonine-protein kinase receptor R3 × 2 （P37023）	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

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 7PPC	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 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 mutation/modification 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
7U5O CRYSTAL STRUCTURE OF THE BONE MORPHOGENETIC PROTEIN RECEPTOR TYPE 2 LIGAND BINDING DOMAIN IN COMPLEX WITH ACTIVIN-B Deposited 2022-03-02	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 27–137（111 aa）	Not recorded	No recorded non-water small molecule	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
7U5O CRYSTAL STRUCTURE OF THE BONE MORPHOGENETIC PROTEIN RECEPTOR TYPE 2 LIGAND BINDING DOMAIN IN COMPLEX WITH ACTIVIN-B Deposited 2022-03-02	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 27–137（111 aa）	Not recorded	No recorded non-water small molecule	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
7U5O CRYSTAL STRUCTURE OF THE BONE MORPHOGENETIC PROTEIN RECEPTOR TYPE 2 LIGAND BINDING DOMAIN IN COMPLEX WITH ACTIVIN-B Deposited 2022-03-02	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain G 27–137（111 aa）	Not recorded	No recorded non-water small molecule	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

5 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	BMPR2_HUMAN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain I； PDBConstruct 1–124； UniProt 27–150 Author chain J； PDBConstruct 1–124； UniProt 27–150 Author chain K； PDBConstruct 1–124； UniProt 27–150 Author chain L； PDBConstruct 1–124； 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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	7ppc
Deposition date deposition_date	2021-09-13
Structure title title	Ternary signalling complex of BMP10 bound to ALK1 and BMPRII
Keywords keywords	BMPRII BMP10 ALK1 Signalling complex, 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	36.07 Å
Radius of gyration Rg (electron density) rg_electron	35.18 Å
Forward intensity I(0) i0	231329000.00
Molecular weight molecular_weight	116550.0 kDa
Excluded volume excluded_volume	143470 Å³
Envelope volume envelope_volume	208530 Å³
Hydration-shell volume shell_volume	49067 Å³
Envelope diameter envelope_diameter	108.3 Å
Shell Rg shell_rg	42.46 Å
Envelope Rg envelope_rg	33.68 Å
Shape Rg shape_rg	35.21 Å
Total Rg total_rg	35.64 Å
Total atoms total_atoms	8126
Residues n_residues	1049
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	104.6 Å
Rg (real space) rg_real	35.80 Å
Rg uncertainty (real space) rg_real_error	0.71 Å
I(0) (real space) i0_real	2.3130e+08
I(0) uncertainty (real space) i0_real_error	3.4060e+06
Rg (reciprocal space) rg_reciprocal	35.97 Å
I(0) (reciprocal space) i0_reciprocal	231400000.0000
Solution quality estimate total_estimate	0.8991
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	49.9 Å
Skewness Skewness skewness	-0.053
Kurtosis Kurtosis kurtosis	-0.602
Angular range angular_range	— – 0.2200 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	11320000.0000
Real-space data points n_real_points	45
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.968; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.796

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Bone morphogenetic protein 10
Molecular weight formula_weight	12177.2 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	8141

NAKGNYCKRTPLYIDFKEIGWDSWIIAPPGYEAYECRGVCNYPLAEHLTPTKHAIIQALVHLKNSQKASKACCVPTKLEPISILYLDKGVVTYKFKYEGMAVSECGCR

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	Homo sapiens

Entity 2 Entity 2 polymer

Description description	Serine/threonine-protein kinase receptor R3
Molecular weight formula_weight	10731.1 kDa
EC 编号 ec_number	2.7.11.30
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

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

DPVKPSRGPLVTCTCESPHCKGPTCRGAWCTVVLVREEGRHPQEHRGCGNLHRELCRGRPTEFVNHYCCDSHLCNHNVSLVLEATQPPSEQPGTDGQ

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	Escherichia coli

Entity 3 Entity 3 polymer

Description description	Bone morphogenetic protein receptor type-2
Molecular weight formula_weight	13908.3 kDa
EC 编号 ec_number	2.7.11.30
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	I,J,K,L

SQNQERLCAFKDPYQQDLGIGESRISHENGTILCSKGSTCYGLWEKSKGDINLVKQGCWSHIGDPQECHYEECVVTTTPPSIQNGTYRFCCCSTDLCNVNFTENFPPPDTTPLSPPHSFNRDET

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	Escherichia coli

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	5

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8. Citations (1)

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Unit-cell length a length_a	63.761 Å
Unit-cell length b length_b	130.387 Å
Unit-cell length c length_c	88.825 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	103.38 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	monoclinic

Resolution resolution	3.600 Å
Low-resolution limit resolution_low	86.410 Å
R factor r_factor	0.2455
R_work r_work	0.2436
R_free r_free	0.2825

fit	/app/data/saxs_computation/pp/7ppc/7ppc.fit
pddf	/app/data/pr_computation/pp/7ppc/7ppc.pr.out
profile	/app/data/saxs_computation/pp/7ppc/7ppc.dat

Ternary signalling complex of BMP10 bound to ALK1 and BMPRII

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

Bone morphogenetic protein 10

State in the Current Structure

Other States of the Same Protein in the Database

Serine/threonine-protein kinase receptor R3

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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)