2yse

Solution structure of the second WW domain from the human membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1. MAGI-1

Method: SOLUTION NMR Dmax: 50.8 Å Quality: GOOD

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

Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1

Homo sapiens

UniProt Q96QZ7

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 355–401 Fragment:WW domain No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;296 K;Ionic strength (raw mmCIF value) 120mM;Pressure ambient NMR sample composition:1.0mM sample U-15N, 13C; 20mM d-Tris-HCl; 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 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.

15 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MAGI1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–54; UniProt 355–401

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 2yse

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2yse
Deposition date deposition_date2007-04-03
Structure title titleSolution structure of the second WW domain from the human membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1. MAGI-1
Keywords keywords;MAGI-1, WW domain, Structural Genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI, PROTEIN BINDING ;; PROTEIN BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.10
Radius of gyration Rg (electron density) rg_electron13.78
Forward intensity I(0) i0258637000.00
Molecular weight molecular_weight131820.0 kDa
Excluded volume excluded_volume163440 ų
Envelope volume envelope_volume24985 ų
Hydration-shell volume shell_volume12659 ų
Envelope diameter envelope_diameter58.4
Shell Rg shell_rg22.73
Envelope Rg envelope_rg18.96
Shape Rg shape_rg13.74
Total Rg total_rg14.16
Total atoms total_atoms18260
Residues n_residues1200
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 dmax50.8
Rg (real space) rg_real14.28
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real2.5860e+08
I(0) uncertainty (real space) i0_real_error3.0210e+06
Rg (reciprocal space) rg_reciprocal14.27
I(0) (reciprocal space) i0_reciprocal258600000.0000
Solution quality estimate total_estimate0.8146
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary49.5
Skewness Skewness skewness0.565
Kurtosis Kurtosis kurtosis-0.110
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha80340.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.663; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.612; Smooth: 0.986

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)