1u7v

Crystal Structure of the phosphorylated Smad2/Smad4 heterotrimeric complex

Method: X-RAY DIFFRACTION Dmax: 78.4 Å Quality: EXCELLENT

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

Mothers against decapentaplegic homolog 2

Homo sapiens

UniProt Q15796

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 270–466 Chain C; UniProt 270–466 Fragment:MH2 and Linker domains Non-standard monomer:Yes (specific site not provided by mmCIF) Mothers against decapentaplegic homolog 4 × 1 (Q13485) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;50 mM Tris-HCl, 0-15 mM magnesium chloride, 5-15% ethanol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.70 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.

8 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SMAD2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–198; UniProt 270–466 Author chain C; PDBConstruct 1–198; UniProt 270–466

Mothers against decapentaplegic homolog 4

Homo sapiens

UniProt Q13485

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 314–549 Fragment:MH2 and Linker domains Mothers against decapentaplegic homolog 2 × 2 (Q15796) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;50 mM Tris-HCl, 0-15 mM magnesium chloride, 5-15% ethanol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.70 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.

9 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SMAD4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–236; UniProt 314–549

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 1u7v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1u7v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1u7v
Deposition date deposition_date2004-08-04
Structure title titleCrystal Structure of the phosphorylated Smad2/Smad4 heterotrimeric complex
Keywords keywordsSmad, TGF-beta, signal transduction, protein complex, phosphorylation, signaling protein; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.33
Radius of gyration Rg (electron density) rg_electron25.18
Forward intensity I(0) i081176200.00
Molecular weight molecular_weight68141.0 kDa
Excluded volume excluded_volume84280 ų
Envelope volume envelope_volume100860 ų
Hydration-shell volume shell_volume32505 ų
Envelope diameter envelope_diameter80.6
Shell Rg shell_rg33.28
Envelope Rg envelope_rg25.07
Shape Rg shape_rg25.16
Total Rg total_rg26.11
Total atoms total_atoms4777
Residues n_residues598
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 dmax78.4
Rg (real space) rg_real26.19
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real8.1180e+07
I(0) uncertainty (real space) i0_real_error1.1220e+06
Rg (reciprocal space) rg_reciprocal26.23
I(0) (reciprocal space) i0_reciprocal81180000.0000
Solution quality estimate total_estimate0.9148
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary77.0
Skewness Skewness skewness0.136
Kurtosis Kurtosis kurtosis-0.583
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19360000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.973; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.975

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1u7va_
Class classb — All beta proteins
Fold Fold foldb.26 — SMAD/FHA domain
Superfamily Superfamily superfamilyb.26.1 — SMAD/FHA domain
Family Family familyb.26.1.1 — SMAD domain
Domain ID domain_idd1u7vb_
Class classb — All beta proteins
Fold Fold foldb.26 — SMAD/FHA domain
Superfamily Superfamily superfamilyb.26.1 — SMAD/FHA domain
Family Family familyb.26.1.1 — SMAD domain
Domain ID domain_idd1u7vc_
Class classb — All beta proteins
Fold Fold foldb.26 — SMAD/FHA domain
Superfamily Superfamily superfamilyb.26.1 — SMAD/FHA domain
Family Family familyb.26.1.1 — SMAD domain

CATH v4.4 (3 domains)

Domain ID domain_id1u7vA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology200 — Tumour Suppressor Smad4
Homologous superfamily homologous superfamily10
Domain ID domain_id1u7vB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology200 — Tumour Suppressor Smad4
Homologous superfamily homologous superfamily10
Domain ID domain_id1u7vC00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology200 — Tumour Suppressor Smad4
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)