2laj

Third WW domain of human Nedd4L in complex with doubly phosphorylated human smad3 derived peptide

Method: SOLUTION NMR Dmax: 37.9 Å Quality: GOOD

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

E3 ubiquitin-protein ligase NEDD4-like

Homo sapiens

UniProt Q96PU5

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 496–535 Fragment:WW 3 domain residues 496-535 Mothers against decapentaplegic homolog 3 × 1 (P84022) SOLUTION NMR NMR measurement conditions:pH 7;285 K;Ionic strength (raw mmCIF value) 0.420;Pressure ambient NMR sample composition:1 mM NEDD4LWW3, 3 mM SMAD3, 20 mM sodium phosphate, 100 mM sodium chloride, 2 mM sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:1 mM [U-100% 15N] NEDD4LWW3, 3 mM SMAD3, 20 mM sodium phosphate, 100 mM sodium chloride, 2 mM sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:1 mM [U-100% 13C; U-100% 15N] NEDD4LWW3, 3 mM SMAD3, 20 mM sodium phosphate, 100 mM sodium chloride, 2 mM sodium azide, 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.

18 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NED4L_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–44; UniProt 496–535

Mothers against decapentaplegic homolog 3

OrganismNot specified

UniProt P84022

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 202–211 Fragment:sequence database residues 202-211 Non-standard monomer:Yes (specific site not provided by mmCIF) E3 ubiquitin-protein ligase NEDD4-like × 1 (Q96PU5) SOLUTION NMR NMR measurement conditions:pH 7;285 K;Ionic strength (raw mmCIF value) 0.420;Pressure ambient NMR sample composition:1 mM NEDD4LWW3, 3 mM SMAD3, 20 mM sodium phosphate, 100 mM sodium chloride, 2 mM sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:1 mM [U-100% 15N] NEDD4LWW3, 3 mM SMAD3, 20 mM sodium phosphate, 100 mM sodium chloride, 2 mM sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:1 mM [U-100% 13C; U-100% 15N] NEDD4LWW3, 3 mM SMAD3, 20 mM sodium phosphate, 100 mM sodium chloride, 2 mM sodium azide, 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.

10 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SMAD3_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–10; UniProt 202–211

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 2laj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2laj
Deposition date deposition_date2011-03-16
Structure title titleThird WW domain of human Nedd4L in complex with doubly phosphorylated human smad3 derived peptide
Keywords keywordsCDK, signal transduction, LIGASE-TRANSCRIPTION REGULATOR complex; LIGASE/TRANSCRIPTION REGULATOR
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier10.77
Radius of gyration Rg (electron density) rg_electron10.53
Forward intensity I(0) i0123062000.00
Molecular weight molecular_weight88972.0 kDa
Excluded volume excluded_volume109320 ų
Envelope volume envelope_volume11022 ų
Hydration-shell volume shell_volume8435 ų
Envelope diameter envelope_diameter39.6
Shell Rg shell_rg16.80
Envelope Rg envelope_rg11.96
Shape Rg shape_rg10.48
Total Rg total_rg10.88
Total atoms total_atoms12045
Residues n_residues720
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 dmax37.9
Rg (real space) rg_real10.77
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real1.2310e+08
I(0) uncertainty (real space) i0_real_error1.5880e+06
Rg (reciprocal space) rg_reciprocal10.77
I(0) (reciprocal space) i0_reciprocal123100000.0000
Solution quality estimate total_estimate0.8432
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary12.9
Skewness Skewness skewness0.312
Kurtosis Kurtosis kurtosis-0.088
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha44680.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.666; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.986

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2lajA01
Class class2 — Mainly Beta
Architecture architecture20 — Single Sheet
Topology topology70 — Ubiquitin Ligase Nedd4; Chain: W;
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)