SAXSdb — 2k3g

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

Bone morphogenetic protein receptor type-1A

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 51–152	Fragment：Extracellular domain (UNP residues 51-152) Mutation：A28G	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 6.3；298 K；Pressure ambient NMR sample composition：1.1 mM [U-99% 15N] Bone Morphogenetic Protein Receptor Type IA, 10 mM potassium phosphate, 0.2 w/v sodium azide, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition：0.5 mM [U-94% 13C; U-98% 15N] Bone Morphogenetic Protein Receptor Type IA, 10 mM potassium phosphate, 0.2 w/v sodium azide, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 2K3G	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1ES7 COMPLEX BETWEEN BMP-2 AND TWO BMP RECEPTOR IA ECTODOMAINS Deposited 2000-04-07	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 55–143（89 aa） Fragment：EXTRACELLULAR DOMAIN Chain D 55–143（89 aa） Fragment：EXTRACELLULAR DOMAIN	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；296 K；sodium acetate, imidazole, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 2.90 Å R-free 0.229
1REW Structural refinement of the complex of bone morphogenetic protein 2 and its type IA receptor Deposited 2003-11-07	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 24–152（129 aa） Fragment：extracellular domain Chain D 24–152（129 aa） Fragment：extracellular domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；280 K；sodium acetate, imidazole, glucose, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 280K	Resolution 1.86 Å R-free 0.229
2GOO Ternary Complex of BMP-2 bound to BMPR-Ia-ECD and ActRII-ECD Deposited 2006-04-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 24–152（129 aa） Fragment：Residues 24-152 Chain E 24–152（129 aa） Fragment：Residues 24-152	Not recorded	NDG 2-acetamido-2-deoxy-alpha-D-glucopyranose × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；4M sodium formate, 100mM Hepes, 3% dioxane, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.259
2H62 Crystal structure of a ternary ligand-receptor complex of BMP-2 Deposited 2006-05-30	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 24–152（129 aa） Fragment：extracellular domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.75；294 K；50% PPG400, 0.1M Bis-Tris, pH 5.75, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 1.85 Å R-free 0.225
2H64 Crystal structure of a ternary ligand-receptor complex of BMP-2 Deposited 2006-05-30	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 24–152（129 aa） Fragment：extracellular domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.75；294 K；30% PEG3350, 0.1M Tris-HCl pH 8.75, 0.2M NH4CH3COO, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 1.92 Å R-free 0.264
2QJ9 Crystal structure analysis of BMP-2 in complex with BMPR-IA variant B1 Deposited 2007-07-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 24–152（129 aa） Fragment：extracellular domain (residues 24-152) Chain D 24–152（129 aa） Fragment：extracellular domain (residues 24-152)	Mutation：K88R,S90T,K92I,A93P,Q94H,L95Q,T98S Mutation：K88R,S90T,K92I,A93P,Q94H,L95Q,T98S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；298 K；0.8M K Na phosphate, 25% ethylene glycol, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.44 Å R-free 0.253
2QJA Crystal structure analysis of BMP-2 in complex with BMPR-IA variant B12 Deposited 2007-07-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 24–152（129 aa） Fragment：extracellular domain (residues 24-152) Chain D 24–152（129 aa） Fragment：extracellular domain (residues 24-152)	Mutation：K88R,S90T,K92I,A93P,Q94H,L95Q,T98S,A74T,M78L,K79G,Y80L Mutation：K88R,S90T,K92I,A93P,Q94H,L95Q,T98S,A74T,M78L,K79G,Y80L	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；298 K；0.8M K Na phosphate, 25% ethylene glycol, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.60 Å R-free 0.254
2QJB Crystal structure analysis of BMP-2 in complex with BMPR-IA variant IA/IB Deposited 2007-07-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 24–152（129 aa） Fragment：extracellular domain (residues 24-152) Chain D 24–152（129 aa） Fragment：extracellular domain (residues 24-152)	Mutation：K88R,S90T,K92I,A93P,Q94H,L95Q,T98S,A74T,M78L,K79G,Y80L,D46E,G42H,A61T,I62M Mutation：K88R,S90T,K92I,A93P,Q94H,L95Q,T98S,A74T,M78L,K79G,Y80L,D46E,G42H,A61T,I62M	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；298 K；0.8M K Na phosphate, 25% ethylene glycol, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.50 Å R-free 0.263
3NH7 Crystal structure of the neutralizing Fab fragment AbD1556 bound to the BMP type I receptor IA Deposited 2010-06-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 24–152（129 aa） Fragment：extracellular domain, UNP residues 24-152	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；294 K；100mM Tris-HCl pH 7.0, 20% (w/v) PEG 8000 and 10% (w/v) glucose , VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.70 Å R-free 0.280
3NH7 Crystal structure of the neutralizing Fab fragment AbD1556 bound to the BMP type I receptor IA Deposited 2010-06-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 24–152（129 aa） Fragment：extracellular domain, UNP residues 24-152	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；294 K；100mM Tris-HCl pH 7.0, 20% (w/v) PEG 8000 and 10% (w/v) glucose , VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.70 Å R-free 0.280
3NH7 Crystal structure of the neutralizing Fab fragment AbD1556 bound to the BMP type I receptor IA Deposited 2010-06-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 24–152（129 aa） Fragment：extracellular domain, UNP residues 24-152	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；294 K；100mM Tris-HCl pH 7.0, 20% (w/v) PEG 8000 and 10% (w/v) glucose , VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.70 Å R-free 0.280
3NH7 Crystal structure of the neutralizing Fab fragment AbD1556 bound to the BMP type I receptor IA Deposited 2010-06-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain D 24–152（129 aa） Fragment：extracellular domain, UNP residues 24-152	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；294 K；100mM Tris-HCl pH 7.0, 20% (w/v) PEG 8000 and 10% (w/v) glucose , VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.70 Å R-free 0.280
3QB4 Crystal structure of a TGF-beta ligand-receptor complex Deposited 2011-01-12	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 24–152（129 aa） Fragment：BMP receptor BMPR-IA, residues 24-152	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；0.1M Hepes pH 7.5, 0.2M NaCl 20% (w/v) PEG3350 , VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.28 Å R-free 0.241
3QB4 Crystal structure of a TGF-beta ligand-receptor complex Deposited 2011-01-12	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 24–152（129 aa） Fragment：BMP receptor BMPR-IA, residues 24-152	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；0.1M Hepes pH 7.5, 0.2M NaCl 20% (w/v) PEG3350 , VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.28 Å R-free 0.241
3QB4 Crystal structure of a TGF-beta ligand-receptor complex Deposited 2011-01-12	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 24–152（129 aa） Fragment：BMP receptor BMPR-IA, residues 24-152 Chain D 24–152（129 aa） Fragment：BMP receptor BMPR-IA, residues 24-152	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；0.1M Hepes pH 7.5, 0.2M NaCl 20% (w/v) PEG3350 , VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.28 Å R-free 0.241

10 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	BMR1A_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–102； UniProt 51–152

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2k3g
Deposition date deposition_date	2008-05-07
Structure title title	NMR structure analysis of a BMP receptor
Keywords keywords	;BMP, receptor, TGF-beta superfamily, ATP-binding, Disease mutation, Glycoprotein, Kinase, Magnesium, Manganese, Membrane, Metal-binding, Nucleotide-binding, Phosphoprotein, Polymorphism, Serine/threonine-protein kinase, Transferase, Transmembrane, SIGNALING PROTEIN ;; SIGNALING PROTEIN
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	17.00 Å
Radius of gyration Rg (electron density) rg_electron	17.57 Å
Forward intensity I(0) i0	899884000.00
Molecular weight molecular_weight	236520.0 kDa
Excluded volume excluded_volume	288700 Å³
Envelope volume envelope_volume	57113 Å³
Hydration-shell volume shell_volume	20481 Å³
Envelope diameter envelope_diameter	87.7 Å
Shell Rg shell_rg	30.43 Å
Envelope Rg envelope_rg	26.14 Å
Shape Rg shape_rg	17.66 Å
Total Rg total_rg	17.58 Å
Total atoms total_atoms	31815
Residues n_residues	2142
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	45.8 Å
Rg (real space) rg_real	15.74 Å
Rg uncertainty (real space) rg_real_error	0.08 Å
I(0) (real space) i0_real	8.5580e+08
I(0) uncertainty (real space) i0_real_error	6.6080e+06
Rg (reciprocal space) rg_reciprocal	17.28 Å
I(0) (reciprocal space) i0_reciprocal	899900000.0000
Solution quality estimate total_estimate	0.6840
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	16.9 Å
Skewness Skewness skewness	0.358
Kurtosis Kurtosis kurtosis	-0.440
Angular range angular_range	— – 0.4700 Å⁻¹
Current regularization parameter α current_alpha	3.5900
Highest regularization parameter α highest_alpha	273300.0000
Real-space data points n_real_points	77
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.012; Oscil: 0.993; Stabil: 0.985; Sysdev: 0.000; Positv: 1.000; Valcen: 0.960; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d2k3ga_
Class class	g — Small proteins
Fold Fold fold	g.7 — Snake toxin-like
Superfamily Superfamily superfamily	g.7.1 — Snake toxin-like
Family Family family	g.7.1.3 — Extracellular domain of cell surface receptors

CATH v4.4 (1 domains)

Domain ID domain_id	2k3gA00
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	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

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

Description description	Bone morphogenetic protein receptor type-1A
Molecular weight formula_weight	11278.7 kDa
EC 编号 ec_number	2.7.11.30
Mutation mutation	A28G
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	31815

来源生物 organism	Homo sapiens
宿主生物 host_organism	Escherichia coli

NMR structure analysis of a BMP receptor

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

Bone morphogenetic protein receptor type-1A

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

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)

fit	/app/data/saxs_computation/k3/2k3g/2k3g.fit
pddf	/app/data/pr_computation/k3/2k3g/2k3g.pr.out
profile	/app/data/saxs_computation/k3/2k3g/2k3g.dat