4wii

HUMAN SPLICING FACTOR, CONSTRUCT 3

Method: X-RAY DIFFRACTION Dmax: 81.8 Å Quality: EXCELLENT

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

Splicing factor, proline- and glutamine-rich

Homo sapiens

UniProt P23246

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 276–535 Chain B; UniProt 276–535 Fragment:UNP RESIDUES 276-535 SO4 SULFATE ION × 1 EDO 1,2-ETHANEDIOL × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;1.9 M AMMONIUM SULFATE, 0.1 M TRIS, 20% ETHYLENE GLYCOL (V/V), PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K Resolution 2.05 Å R-free 0.235

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.

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

View Construct and Data Evidence
UniProt name SFPQ_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–263; UniProt 276–535 Author chain B; PDBConstruct 4–263; UniProt 276–535

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 4wii

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4wii
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4wii
Deposition date deposition_date2014-09-26
Structure title titleHUMAN SPLICING FACTOR, CONSTRUCT 3
Keywords keywordsRRM, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.64
Radius of gyration Rg (electron density) rg_electron25.63
Forward intensity I(0) i057392500.00
Molecular weight molecular_weight57688.0 kDa
Excluded volume excluded_volume71861 ų
Envelope volume envelope_volume92922 ų
Hydration-shell volume shell_volume30630 ų
Envelope diameter envelope_diameter86.9
Shell Rg shell_rg32.50
Envelope Rg envelope_rg25.23
Shape Rg shape_rg25.63
Total Rg total_rg26.40
Total atoms total_atoms4060
Residues n_residues498
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 dmax81.8
Rg (real space) rg_real26.49
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real5.7390e+07
I(0) uncertainty (real space) i0_real_error8.2780e+05
Rg (reciprocal space) rg_reciprocal26.54
I(0) (reciprocal space) i0_reciprocal57390000.0000
Solution quality estimate total_estimate0.9105
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary80.5
Skewness Skewness skewness0.112
Kurtosis Kurtosis kurtosis-0.582
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6506000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.954; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.973

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id4wiiA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily330 — RRM (RNA recognition motif) domain
Domain ID domain_id4wiiA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily330 — RRM (RNA recognition motif) domain
Domain ID domain_id4wiiA03
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily1170
Domain ID domain_id4wiiB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily330 — RRM (RNA recognition motif) domain
Domain ID domain_id4wiiB02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily330 — RRM (RNA recognition motif) domain
Domain ID domain_id4wiiB03
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily1170

8. Citations (1)

9. Files and Curves (10)