3bk3

Crystal structure of the complex of BMP-2 and the first Von Willebrand domain type C of Crossveinless-2

Method: X-RAY DIFFRACTION Dmax: 116.4 Å Quality: REASONABLE

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

Bone morphogenetic protein 2

Homo sapiens

UniProt P12643

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 283–396 Chain B; UniProt 283–396 Mutation:F41M, Y91M Crossveinless 2 × 2 (Q5D734) 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
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 283–396 Chain B; UniProt 283–396 Mutation:F41M, Y91M Crossveinless 2 × 2 (Q5D734) 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
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 283–396 Mutation:F41M, Y91M Crossveinless 2 × 1 (Q5D734) 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
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 283–396 Mutation:F41M, Y91M Crossveinless 2 × 1 (Q5D734) 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

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.

19 other PDB entries and 23 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 1–114; UniProt 283–396 Author chain B; PDBConstruct 1–114; UniProt 283–396

Crossveinless 2

Danio rerio

UniProt Q5D734

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 C; UniProt 28–93 Chain D; UniProt 28–93 Fragment:VWC1 CV-2, VWC domain 1, UNP residues 28-93 Bone morphogenetic protein 2 × 2 (P12643) 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
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 28–93 Chain D; UniProt 28–93 Fragment:VWC1 CV-2, VWC domain 1, UNP residues 28-93 Bone morphogenetic protein 2 × 2 (P12643) 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
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 28–93 Fragment:VWC1 CV-2, VWC domain 1, UNP residues 28-93 Bone morphogenetic protein 2 × 1 (P12643) 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
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 28–93 Fragment:VWC1 CV-2, VWC domain 1, UNP residues 28-93 Bone morphogenetic protein 2 × 1 (P12643) 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

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q5D734_DANRE
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 2–67; UniProt 28–93 Author chain D; PDBConstruct 2–67; UniProt 28–93

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

SAXS scattering curve SAXS Profile

SAXS profile for 3bk3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3bk3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3bk3
Deposition date deposition_date2007-12-05
Structure title titleCrystal structure of the complex of BMP-2 and the first Von Willebrand domain type C of Crossveinless-2
Keywords keywords;TGF-beta superfamily, BMP modulator proteins, Chordin, BMP inhibitor, Chondrogenesis, Cleavage on pair of basic residues, Cytokine, Developmental protein, Differentiation, Glycoprotein, Growth factor, Osteogenesis, Polymorphism, Secreted, Hormone-growth Factor COMPLEX ;; Hormone/growth Factor
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.39
Radius of gyration Rg (electron density) rg_electron29.48
Forward intensity I(0) i025907300.00
Molecular weight molecular_weight37344.0 kDa
Excluded volume excluded_volume45889 ų
Envelope volume envelope_volume67191 ų
Hydration-shell volume shell_volume20855 ų
Envelope diameter envelope_diameter122.6
Shell Rg shell_rg32.85
Envelope Rg envelope_rg30.90
Shape Rg shape_rg29.39
Total Rg total_rg30.08
Total atoms total_atoms2588
Residues n_residues342
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax116.4
Rg (real space) rg_real29.90
Rg uncertainty (real space) rg_real_error1.26
I(0) (real space) i0_real2.5910e+07
I(0) uncertainty (real space) i0_real_error4.4720e+05
Rg (reciprocal space) rg_reciprocal29.68
I(0) (reciprocal space) i0_reciprocal25900000.0000
Solution quality estimate total_estimate0.7213
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.7
Skewness Skewness skewness0.735
Kurtosis Kurtosis kurtosis0.254
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3242000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.395; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.220; Smooth: 0.969

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3bk3a_
Class classg — Small proteins
Fold Fold foldg.17 — Cystine-knot cytokines
Superfamily Superfamily superfamilyg.17.1 — Cystine-knot cytokines
Family Family familyg.17.1.2 — Transforming growth factor (TGF)-beta
Domain ID domain_idd3bk3b_
Class classg — Small proteins
Fold Fold foldg.17 — Cystine-knot cytokines
Superfamily Superfamily superfamilyg.17.1 — Cystine-knot cytokines
Family Family familyg.17.1.2 — Transforming growth factor (TGF)-beta

CATH v4.4 (4 domains)

Domain ID domain_id3bk3A00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id3bk3B00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id3bk3C00
Class class6 — Special
Architecture architecture20 — Other non-globular
Topology topology200 — Defensin A-like
Homologous superfamily homologous superfamily20
Domain ID domain_id3bk3D00
Class class6 — Special
Architecture architecture20 — Other non-globular
Topology topology200 — Defensin A-like
Homologous superfamily homologous superfamily20

8. Citations (1)

9. Files and Curves (10)