2jxw

Solution Structure of the Tandem WW Domains of FBP21

Method: SOLUTION NMR Dmax: 59.0 Å Quality: GOOD

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

WW domain-binding protein 4

Homo sapiens

UniProt O75554

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 122–196 Fragment:WW Domian No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;293 K;Pressure 1 NMR measurement conditions:pH 6.5;298 K;Pressure 1 NMR sample composition:1.0mM [U-99% 13C; U-99% 15N] FBP21; 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.5mM [U-99% 15N] FBP21; 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 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WBP4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–75; UniProt 122–196

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 2jxw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2jxw
Deposition date deposition_date2007-11-30
Structure title titleSolution Structure of the Tandem WW Domains of FBP21
Keywords keywords;WW domain containing protein, WW domain, FBP21, WBP4, Metal-binding, mRNA processing, mRNA splicing, Nucleus, Polymorphism, Spliceosome, Zinc, Zinc-finger, FORMIN BINDING PROTEIN ;; FORMIN BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier16.41
Radius of gyration Rg (electron density) rg_electron16.15
Forward intensity I(0) i0441606000.00
Molecular weight molecular_weight173450.0 kDa
Excluded volume excluded_volume214670 ų
Envelope volume envelope_volume53254 ų
Hydration-shell volume shell_volume22577 ų
Envelope diameter envelope_diameter65.8
Shell Rg shell_rg26.31
Envelope Rg envelope_rg19.43
Shape Rg shape_rg16.12
Total Rg total_rg16.56
Total atoms total_atoms23460
Residues n_residues1500
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 dmax59.0
Rg (real space) rg_real16.43
Rg uncertainty (real space) rg_real_error0.52
I(0) (real space) i0_real4.4160e+08
I(0) uncertainty (real space) i0_real_error5.0070e+06
Rg (reciprocal space) rg_reciprocal16.43
I(0) (reciprocal space) i0_reciprocal441600000.0000
Solution quality estimate total_estimate0.7678
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary53.7
Skewness Skewness skewness0.326
Kurtosis Kurtosis kurtosis-0.412
Angular range angular_range— – 0.4850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10080000.0000
Real-space data points n_real_points79
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.725; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.802; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2jxwA00
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)