1lx5

Crystal Structure of the BMP7/ActRII Extracellular Domain Complex

Method: X-RAY DIFFRACTION Dmax: 76.5 Å Quality: GOOD

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

bone morphogenetic protein 7

Homo sapiens

UniProt P18075

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 2 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 293–431 Not recorded Activin Type II Receptor × 2 (P27038) ;alpha-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-4)][alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;296 K;1M sodium acetate, 0.1M imidazole, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 296K Resolution 3.30 Å R-free 0.279

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BMP7_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–139; UniProt 293–431

Activin Type II Receptor

Mus musculus

UniProt P27038

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 2 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 20–121 Fragment:Extracellular Ligand Binding Domain, C-terminal truncation bone morphogenetic protein 7 × 2 (P18075) ;alpha-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-4)][alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;296 K;1M sodium acetate, 0.1M imidazole, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 296K Resolution 3.30 Å R-free 0.279

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.

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AVR2_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–102; UniProt 20–121

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 1lx5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1lx5
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1lx5
Deposition date deposition_date2002-06-04
Structure title titleCrystal Structure of the BMP7/ActRII Extracellular Domain Complex
Keywords keywordsLIGAND-RECEPTOR COMPLEX, GROWTH FACTOR-GROWTH FACTOR RECEPTOR COMPLEX; GROWTH FACTOR/GROWTH FACTOR RECEPTOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.43
Radius of gyration Rg (electron density) rg_electron21.28
Forward intensity I(0) i011412400.00
Molecular weight molecular_weight24266.0 kDa
Excluded volume excluded_volume29894 ų
Envelope volume envelope_volume37331 ų
Hydration-shell volume shell_volume16264 ų
Envelope diameter envelope_diameter78.1
Shell Rg shell_rg25.55
Envelope Rg envelope_rg21.53
Shape Rg shape_rg21.30
Total Rg total_rg21.82
Total atoms total_atoms1695
Residues n_residues198
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 dmax76.5
Rg (real space) rg_real21.63
Rg uncertainty (real space) rg_real_error0.73
I(0) (real space) i0_real1.1410e+07
I(0) uncertainty (real space) i0_real_error1.5670e+05
Rg (reciprocal space) rg_reciprocal21.60
I(0) (reciprocal space) i0_reciprocal11410000.0000
Solution quality estimate total_estimate0.8166
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.5
Skewness Skewness skewness0.556
Kurtosis Kurtosis kurtosis-0.176
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1070000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.690; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.690; Smooth: 0.851

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1lx5a_
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_idd1lx5b_
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 (2 domains)

Domain ID domain_id1lx5A00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id1lx5B00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology60 — CD59
Homologous superfamily homologous superfamily10 — CD59

8. Citations (1)

9. Files and Curves (10)