6sf3

Bone morphogenetic protein 10 (BMP10) in complex with extracellular domain of activin receptor-like kinase 1 (ALK1) at 2.3 Angstrom

Method: X-RAY DIFFRACTION D_max: 74.8 Å Quality: GOOD

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

Serine/threonine-protein kinase receptor R3

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 × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 21–118	Not recorded	Bone morphogenetic protein 10 × 2 （O95393）	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

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 6SF3	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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 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 mutation/modification Different oligomeric state 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
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 E 22–118（97 aa） Chain F 22–118（97 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 G 22–118（97 aa） Chain H 22–118（97 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

6 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ACVL1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–98； UniProt 21–118

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 B； UniProt 317–424	Not recorded	Serine/threonine-protein kinase receptor R3 × 2 （P37023）	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

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 6SF3	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 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
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 construct Different mutation/modification 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 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
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 A 317–424（108 aa） 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 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 C 317–424（108 aa） Chain D 317–424（108 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；294.15 K；20% PEG 3350 0.2 M Calcium acetate hydrate	Resolution 3.60 Å R-free 0.282
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 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	BMP10_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–108； UniProt 317–424

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	6sf3
Deposition date deposition_date	2019-07-31
Structure title title	Bone morphogenetic protein 10 (BMP10) in complex with extracellular domain of activin receptor-like kinase 1 (ALK1) at 2.3 Angstrom
Keywords keywords	BMP10, ALK1, complex, signalling, TGFbeta, BMP, CYTOKINE; CYTOKINE
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	21.25 Å
Radius of gyration Rg (electron density) rg_electron	21.63 Å
Forward intensity I(0) i0	8093960.00
Molecular weight molecular_weight	20330.0 kDa
Excluded volume excluded_volume	25180 Å³
Envelope volume envelope_volume	32526 Å³
Hydration-shell volume shell_volume	14187 Å³
Envelope diameter envelope_diameter	76.2 Å
Shell Rg shell_rg	25.68 Å
Envelope Rg envelope_rg	21.88 Å
Shape Rg shape_rg	21.70 Å
Total Rg total_rg	22.05 Å
Total atoms total_atoms	1419
Residues n_residues	180
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	74.8 Å
Rg (real space) rg_real	21.55 Å
Rg uncertainty (real space) rg_real_error	0.74 Å
I(0) (real space) i0_real	8.0940e+06
I(0) uncertainty (real space) i0_real_error	1.2860e+05
Rg (reciprocal space) rg_reciprocal	21.49 Å
I(0) (reciprocal space) i0_reciprocal	8094000.0000
Solution quality estimate total_estimate	0.8012
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	20.9 Å
Skewness Skewness skewness	0.617
Kurtosis Kurtosis kurtosis	-0.236
Angular range angular_range	— – 0.3750 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	756400.0000
Real-space data points n_real_points	69
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.643; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.573; Smooth: 0.910

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Serine/threonine-protein kinase receptor R3
Molecular weight formula_weight	10788.1 kDa
EC 编号 ec_number	2.7.11.30
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1470

GDPVKPSRGPLVTCTCESPHCKGPTCRGAWCTVVLVREEGRHPQEHRGCGNLHRELCRGRPTEFVNHYCCDSHLCNHNVSLVLEATQPPSEQPGTDGQ

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 2 Entity 2 polymer

Description description	Bone morphogenetic protein 10
Molecular weight formula_weight	12177.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

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 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	24

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d6sf3b_
Class class	g — Small proteins
Fold Fold fold	g.17 — Cystine-knot cytokines
Superfamily Superfamily superfamily	g.17.1 — Cystine-knot cytokines
Family Family family	g.17.1.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id	6sf3A00
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	60 — CD59
Homologous superfamily homologous superfamily	10 — CD59

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8. Citations (1)

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Unit-cell length a length_a	58.269 Å
Unit-cell length b length_b	58.269 Å
Unit-cell length c length_c	311.435 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	P 65 2 2
Space-group number int_tables_number	179
Crystal system crystal_system	hexagonal

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	51.906 Å
R factor r_factor	0.2155
R_work r_work	0.2140
R_free r_free	0.2433

fit	/app/data/saxs_computation/sf/6sf3/6sf3.fit
pddf	/app/data/pr_computation/sf/6sf3/6sf3.pr.out
profile	/app/data/saxs_computation/sf/6sf3/6sf3.dat

Bone morphogenetic protein 10 (BMP10) in complex with extracellular domain of activin receptor-like kinase 1 (ALK1) at 2.3 Angstrom

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

Serine/threonine-protein kinase receptor R3

State in the Current Structure

Other States of the Same Protein in the Database

Bone morphogenetic protein 10

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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)