2lb0

Structure of the first WW domain of human Smurf1 in complex with a di-phosphorylated human Smad1 derived peptide

Method: SOLUTION NMR Dmax: 33.2 Å Quality: REASONABLE

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

E3 ubiquitin-protein ligase SMURF1

Homo sapiens

UniProt Q9HCE7

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 235–267 Fragment:residues 235-267 Mothers against decapentaplegic homolog 1 × 1 (Q15797) SOLUTION NMR NMR measurement conditions:pH 7;285 K;Ionic strength (raw mmCIF value) 0.420;Pressure ambient NMR sample composition:1 mM NEDD4LWW3-1, 3 mM SMAD3-2, 20 mM sodium phosphate-3, 100 mM sodium chloride-4, 2 mM sodium azide-5, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:1 mM [U-100% 15N] NEDD4LWW3-6, 3 mM SMAD3-7, 20 mM sodium phosphate-8, 100 mM sodium chloride-9, 2 mM sodium azide-10, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:1 mM [U-100% 13C; U-100% 15N] NEDD4LWW3-11, 3 mM SMAD3-12, 20 mM sodium phosphate-13, 100 mM sodium chloride-14, 2 mM sodium azide-15, 90% H2O/10% D2O | 90% H2O/10% D2O Resolution not provided

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.

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

View Construct and Data Evidence
UniProt name SMUF1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–36; UniProt 235–267

Mothers against decapentaplegic homolog 1

OrganismNot specified

UniProt Q15797

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 208–217 Fragment:residues 208-217 Non-standard monomer:Yes (specific site not provided by mmCIF) E3 ubiquitin-protein ligase SMURF1 × 1 (Q9HCE7) SOLUTION NMR NMR measurement conditions:pH 7;285 K;Ionic strength (raw mmCIF value) 0.420;Pressure ambient NMR sample composition:1 mM NEDD4LWW3-1, 3 mM SMAD3-2, 20 mM sodium phosphate-3, 100 mM sodium chloride-4, 2 mM sodium azide-5, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:1 mM [U-100% 15N] NEDD4LWW3-6, 3 mM SMAD3-7, 20 mM sodium phosphate-8, 100 mM sodium chloride-9, 2 mM sodium azide-10, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:1 mM [U-100% 13C; U-100% 15N] NEDD4LWW3-11, 3 mM SMAD3-12, 20 mM sodium phosphate-13, 100 mM sodium chloride-14, 2 mM sodium azide-15, 90% H2O/10% D2O | 90% H2O/10% D2O Resolution not provided

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.

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

View Construct and Data Evidence
UniProt name SMAD1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–10; UniProt 208–217

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 2lb0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2lb0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2lb0
Deposition date deposition_date2011-03-22
Structure title titleStructure of the first WW domain of human Smurf1 in complex with a di-phosphorylated human Smad1 derived peptide
Keywords keywordsSMURF, SMAD, CDK, signal transduction, SIGNALING PROTEIN-TRANSCRIPTION complex; SIGNALING PROTEIN/TRANSCRIPTION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier10.28
Radius of gyration Rg (electron density) rg_electron10.22
Forward intensity I(0) i0194512000.00
Molecular weight molecular_weight106160.0 kDa
Excluded volume excluded_volume127770 ų
Envelope volume envelope_volume9900 ų
Hydration-shell volume shell_volume7852 ų
Envelope diameter envelope_diameter36.3
Shell Rg shell_rg16.41
Envelope Rg envelope_rg11.64
Shape Rg shape_rg10.19
Total Rg total_rg10.47
Total atoms total_atoms14091
Residues n_residues861
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 dmax33.2
Rg (real space) rg_real10.25
Rg uncertainty (real space) rg_real_error0.26
I(0) (real space) i0_real1.9450e+08
I(0) uncertainty (real space) i0_real_error2.3120e+06
Rg (reciprocal space) rg_reciprocal10.25
I(0) (reciprocal space) i0_reciprocal194500000.0000
Solution quality estimate total_estimate0.7384
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary12.2
Skewness Skewness skewness0.150
Kurtosis Kurtosis kurtosis-0.414
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha42090.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.836; Stabil: 1.000; Sysdev: 0.368; Positv: 1.000; Valcen: 1.000; Smooth: 0.982

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)