2qja

Crystal structure analysis of BMP-2 in complex with BMPR-IA variant B12

Method: X-RAY DIFFRACTION Dmax: 78.3 Å Quality: GOOD

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 Fragment:mature part (residues 283-396) Bone morphogenetic protein receptor type IA × 2 (P36894) 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

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 26 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 3–116; UniProt 283–396 Author chain B; PDBConstruct 3–116; UniProt 283–396

Bone morphogenetic protein receptor type IA

Homo sapiens

UniProt P36894

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 24–152 Chain D; UniProt 24–152 Fragment:extracellular domain (residues 24-152) Mutation:K88R,S90T,K92I,A93P,Q94H,L95Q,T98S,A74T,M78L,K79G,Y80L Bone morphogenetic protein 2 × 2 (P12643) 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

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.

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 2
Chains and sequence ranges Author chain C; PDBConstruct 7–135; UniProt 24–152 Author chain D; PDBConstruct 7–135; UniProt 24–152

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.

SAXS scattering curve SAXS Profile

SAXS profile for 2qja

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2qja
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2qja
Deposition date deposition_date2007-07-06
Structure title titleCrystal structure analysis of BMP-2 in complex with BMPR-IA variant B12
Keywords keywords;ligand-receptor complex, Chondrogenesis, Cleavage on pair of basic residues, Cytokine, Developmental protein, Differentiation, Glycoprotein, Growth factor, Osteogenesis, ATP-binding, Disease mutation, Kinase, Magnesium, Manganese, Membrane, Metal-binding, Nucleotide-binding, Phosphorylation, Serine/threonine-protein kinase, Transferase, Transmembrane, Cytokine-Receptor COMPLEX ;; Cytokine/Receptor
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.30
Radius of gyration Rg (electron density) rg_electron23.98
Forward intensity I(0) i034493500.00
Molecular weight molecular_weight42910.0 kDa
Excluded volume excluded_volume52723 ų
Envelope volume envelope_volume67630 ų
Hydration-shell volume shell_volume23916 ų
Envelope diameter envelope_diameter83.5
Shell Rg shell_rg30.66
Envelope Rg envelope_rg24.12
Shape Rg shape_rg24.01
Total Rg total_rg24.71
Total atoms total_atoms2993
Residues n_residues386
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 dmax78.3
Rg (real space) rg_real24.35
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real3.4490e+07
I(0) uncertainty (real space) i0_real_error4.9590e+05
Rg (reciprocal space) rg_reciprocal24.34
I(0) (reciprocal space) i0_reciprocal34490000.0000
Solution quality estimate total_estimate0.8912
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.1
Skewness Skewness skewness0.368
Kurtosis Kurtosis kurtosis-0.488
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5684000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.879; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.955; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd2qjaa_
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_idd2qjab_
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_idd2qjac_
Class classg — Small proteins
Fold Fold foldg.7 — Snake toxin-like
Superfamily Superfamily superfamilyg.7.1 — Snake toxin-like
Family Family familyg.7.1.3 — Extracellular domain of cell surface receptors
Domain ID domain_idd2qjad_
Class classg — Small proteins
Fold Fold foldg.7 — Snake toxin-like
Superfamily Superfamily superfamilyg.7.1 — Snake toxin-like
Family Family familyg.7.1.3 — Extracellular domain of cell surface receptors

CATH v4.4 (4 domains)

Domain ID domain_id2qjaA00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id2qjaB00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id2qjaC00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology60 — CD59
Homologous superfamily homologous superfamily10 — CD59
Domain ID domain_id2qjaD00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology60 — CD59
Homologous superfamily homologous superfamily10 — CD59

8. Citations (1)

9. Files and Curves (10)