SAXSdb — 1reu

▼

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

bone morphogenetic protein 2

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 294–396	Fragment：mature part Mutation：L51P	MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 4	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5；298 K；lithium sulfate, tert-butanol, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.65 Å R-free 0.235
2	Protein homooligomer Homooligomer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain A； UniProt 294–396	Fragment：mature part Mutation：L51P	MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 12	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5；298 K；lithium sulfate, tert-butanol, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.65 Å R-free 0.235

Other States of the Same Protein in the Database

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

Other PDB	Difference from Current Entry 1REU	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 ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 283–396（114 aa） Chain C 283–396（114 aa）	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 ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 283–396（114 aa） Fragment：mature part Chain B 283–396（114 aa） Fragment：mature part	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 conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 283–396（114 aa） Fragment：Residues 283-396 Chain D 283–396（114 aa） Fragment：Residues 283-396	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 ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 283–396（114 aa） Chain B 283–396（114 aa）	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 ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 283–396（114 aa）	Mutation：L100K, N102D	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 ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 283–396（114 aa） Fragment：mature part (residues 283-396) Chain B 283–396（114 aa） Fragment：mature part (residues 283-396)	Not recorded	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 ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 283–396（114 aa） Fragment：mature part (residues 283-396) Chain B 283–396（114 aa） Fragment：mature part (residues 283-396)	Not recorded	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 conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 283–396（114 aa） Fragment：mature part (residues 283-396) Chain B 283–396（114 aa） Fragment：mature part (residues 283-396)	Not recorded	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
3BK3 Crystal structure of the complex of BMP-2 and the first Von Willebrand domain type C of Crossveinless-2 Deposited 2007-12-05	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 283–396（114 aa） Chain B 283–396（114 aa）	Mutation：F41M, Y91M Mutation：F41M, Y91M	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；2.2M ammonium phosphate, 0.1M Tris pH 7.5, 8% glycerol, 5% sucrose, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.70 Å R-free 0.245
3BK3 Crystal structure of the complex of BMP-2 and the first Von Willebrand domain type C of Crossveinless-2 Deposited 2007-12-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 283–396（114 aa） Chain B 283–396（114 aa）	Mutation：F41M, Y91M Mutation：F41M, Y91M	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；2.2M ammonium phosphate, 0.1M Tris pH 7.5, 8% glycerol, 5% sucrose, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.70 Å R-free 0.245
3BK3 Crystal structure of the complex of BMP-2 and the first Von Willebrand domain type C of Crossveinless-2 Deposited 2007-12-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 283–396（114 aa）	Mutation：F41M, Y91M	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；2.2M ammonium phosphate, 0.1M Tris pH 7.5, 8% glycerol, 5% sucrose, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.70 Å R-free 0.245
3BK3 Crystal structure of the complex of BMP-2 and the first Von Willebrand domain type C of Crossveinless-2 Deposited 2007-12-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 283–396（114 aa）	Mutation：F41M, Y91M	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；2.2M ammonium phosphate, 0.1M Tris pH 7.5, 8% glycerol, 5% sucrose, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.70 Å R-free 0.245
3BMP HUMAN BONE MORPHOGENETIC PROTEIN-2 (BMP-2) Deposited 1999-03-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 283–396（114 aa）	Not recorded	MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.4；CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 100 MM LITHIUM SULFATE, 12% TERT-BUTANOL, 50 MM CITRATE, PH 5.4	Resolution 2.70 Å R-free 0.278
4N1D Nodal/BMP2 chimera NB250 Deposited 2013-10-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 283–305（23 aa） Chain A 362–396（35 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；288 K；0.2M NaCl, 0.1 M Na acetate pH 4.6, 30% 2-Methyl-2,4-pentanediol, VAPOR DIFFUSION, HANGING DROP, temperature 288K	Resolution 1.91 Å R-free 0.204
4UHY Crystal structure of the human RGMA-BMP2 complex Deposited 2015-03-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 283–396（114 aa） Fragment：C-TERMINAL DOMAIN SIGNALING DOMAIN, RESIDUES 283-396 Chain B 283–396（114 aa） Fragment：C-TERMINAL DOMAIN SIGNALING DOMAIN, RESIDUES 283-396	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 4；0.1 M CITRIC ACID, PH 4.0, 20% (V/V) 2-METHYL-2,4-PENTANEDIOL (MPD), 0.2 M GLYCINE	Resolution 3.20 Å R-free 0.264
4UHZ Crystal structure of the human RGMB-BMP2 complex, crystal form 1 Deposited 2015-03-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 283–396（114 aa） Fragment：C-TERMINAL DOMAIN SIGNALING DOMAIN, RESIDUES 283-396	Not recorded	SO4 SULFATE ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions 2 M AMMONIUM SULPHATE, 8% (V/V) 2,5- HEXANEDIOL	Resolution 2.85 Å R-free 0.229
4UI0 Crystal structure of the human RGMB-BMP2 complex, crystal form 2 Deposited 2015-03-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 283–396（114 aa） Fragment：C-TERMINAL DOMAIN SIGNALING DOMAIN, RESIDUES 283-396 Chain B 283–396（114 aa） Fragment：C-TERMINAL DOMAIN SIGNALING DOMAIN, RESIDUES 283-396	Not recorded	MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 FLC CITRATE ANION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 4；0.08 M CITRIC ACID PH 4.0, 15% (V/V) MPD	Resolution 2.80 Å R-free 0.267
4UI1 Crystal structure of the human RGMC-BMP2 complex Deposited 2015-03-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 283–396（114 aa） Fragment：C-TERMINAL DOMAIN SIGNALING DOMAIN, RESIDUES 283-396	Not recorded	NO3 NITRATE ION × 2 CL CHLORIDE ION × 2 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；20% (W/V) PEG3350, 0.2 M AMMONIUM NITRATE, PH 7.5	Resolution 2.35 Å R-free 0.238
4UI1 Crystal structure of the human RGMC-BMP2 complex Deposited 2015-03-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 283–396（114 aa） Fragment：C-TERMINAL DOMAIN SIGNALING DOMAIN, RESIDUES 283-396	Not recorded	NO3 NITRATE ION × 4 EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；20% (W/V) PEG3350, 0.2 M AMMONIUM NITRATE, PH 7.5	Resolution 2.35 Å R-free 0.238
4UI2 Crystal structure of the ternary RGMB-BMP2-NEO1 complex Deposited 2015-03-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 8 PDB declaration: octameric	Chain B 283–396（114 aa） Fragment：C-TERMINAL DOMAIN SIGNALING DOMAIN	Not recorded	SRT S,R MESO-TARTARIC ACID × 6 ACT ACETATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；0.1 M TRIS-HCL PH 8.5, 1.5 M AMMONIUM SULPHATE, 12% (V/V) GLYCEROL	Resolution 3.15 Å R-free 0.236
6OMN Glycosylated BMP2 homodimer Deposited 2019-04-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain E 289–396（108 aa） Chain F 289–396（108 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；100mM TrisHCl pH 8.5, 100mM NaCl, 12% MPD	Resolution 2.68 Å R-free 0.243
6OMN Glycosylated BMP2 homodimer Deposited 2019-04-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain G 289–396（108 aa） Chain H 289–396（108 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；100mM TrisHCl pH 8.5, 100mM NaCl, 12% MPD	Resolution 2.68 Å R-free 0.243
7AG0 Complex between the bone morphogenetic protein 2 and its antagonist Noggin Deposited 2020-09-21	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 283–396（114 aa）	Not recorded	GOL GLYCEROL × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；293 K；1.4 M NaKPO4	Resolution 3.10 Å R-free 0.280
8E3G BMP2/GDF5 heterodimer Deposited 2022-08-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 283–396（114 aa）	Not recorded	GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；Tris, magnesium formate	Resolution 2.80 Å R-free 0.234
8E3G BMP2/GDF5 heterodimer Deposited 2022-08-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 283–396（114 aa）	Not recorded	GOL GLYCEROL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；Tris, magnesium formate	Resolution 2.80 Å R-free 0.234

19 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	BMP2_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–103； UniProt 294–396

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1reu
Deposition date deposition_date	2003-11-07
Structure title title	Structure of the bone morphogenetic protein 2 mutant L51P
Keywords keywords	TGF-beta fold, HORMONE-GROWTH FACTOR COMPLEX; HORMONE/GROWTH FACTOR
Experimental Method method	X-RAY DIFFRACTION

▼

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

Radius of gyration Rg (Guinier) rg_guinier	18.40 Å
Radius of gyration Rg (electron density) rg_electron	18.39 Å
Forward intensity I(0) i0	2713200.00
Molecular weight molecular_weight	11718.0 kDa
Excluded volume excluded_volume	14601 Å³
Envelope volume envelope_volume	18587 Å³
Hydration-shell volume shell_volume	9435 Å³
Envelope diameter envelope_diameter	62.6 Å
Shell Rg shell_rg	22.31 Å
Envelope Rg envelope_rg	18.53 Å
Shape Rg shape_rg	18.41 Å
Total Rg total_rg	19.04 Å
Total atoms total_atoms	820
Residues n_residues	103
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

▼

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

Maximum dimension Dmax dmax	63.4 Å
Rg (real space) rg_real	18.60 Å
Rg uncertainty (real space) rg_real_error	0.48 Å
I(0) (real space) i0_real	2.7130e+06
I(0) uncertainty (real space) i0_real_error	3.5300e+04
Rg (reciprocal space) rg_reciprocal	18.57 Å
I(0) (reciprocal space) i0_reciprocal	2713000.0000
Solution quality estimate total_estimate	0.8236
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	15.6 Å
Skewness Skewness skewness	0.461
Kurtosis Kurtosis kurtosis	-0.561
Angular range angular_range	— – 0.4300 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	237900.0000
Real-space data points n_real_points	74
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.744; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.487; Smooth: 0.984

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	bone morphogenetic protein 2
Molecular weight formula_weight	11498.1 kDa
Mutation mutation	L51P
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	833

SSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPPADHLNSTNHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR

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 non-polymer

Description description	(4S)-2-METHYL-2,4-PENTANEDIOL
Molecular weight formula_weight	118.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	13

▼

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1reua_
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.17.1.2 — Transforming growth factor (TGF)-beta

CATH v4.4 (1 domains)

Domain ID domain_id	1reuA00
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily	10 — Cystine-knot cytokines

▶

8. Citations (3)

▶

Unit-cell length a length_a	94.292 Å
Unit-cell length b length_b	94.292 Å
Unit-cell length c length_c	102.882 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	18

Space group space_group	H 3 2
Space-group number int_tables_number	155
Crystal system crystal_system	—

Resolution resolution	2.650 Å
Low-resolution limit resolution_low	19.760 Å
R factor r_factor	0.2151
R_work r_work	0.2150
R_free r_free	0.2350

fit	/app/data/saxs_computation/re/1reu/1reu.fit
pddf	/app/data/pr_computation/re/1reu/1reu.pr.out
profile	/app/data/saxs_computation/re/1reu/1reu.dat

Structure of the bone morphogenetic protein 2 mutant L51P

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

bone morphogenetic protein 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