5ev3

Structure III of Intact U2AF65 Recognizing the 3' Splice Site Signal

Method: X-RAY DIFFRACTION Dmax: 59.2 Å Quality: GOOD

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

Splicing factor U2AF 65 kDa subunit

Homo sapiens

UniProt P26368

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–DNA Monomer Protein × 1 DNA 1 PDB declaration: dimeric(2) Consistent with all polymer counts Chain A; UniProt 141–341 Fragment:UNP residues 141-341 ;DNA/RNA (5'-R(P*UP*U)-D(P*U)-R(P*UP*U)-D(P*(BRU)P*UP*U)-3') ; × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;1M Succinic Acid, 0.1M, 1% PEG MME 2000 Resolution 1.50 Å R-free 0.186

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.

39 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name U2AF2_HUMAN
Isoform P26368-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–201; UniProt 141–341

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 5ev3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5ev3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5ev3
Deposition date deposition_date2015-11-19
Structure title titleStructure III of Intact U2AF65 Recognizing the 3' Splice Site Signal
Keywords keywordsPROTEIN-RNA COMPLEX, RNA SPLICING FACTOR, RNA RECOGNITION MOTIF, POLYPYRIMIDINE TRACT, RNA BINDING PROTEIN-RNA complex; RNA BINDING PROTEIN/RNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.51
Radius of gyration Rg (electron density) rg_electron17.67
Forward intensity I(0) i011229700.00
Molecular weight molecular_weight23583.0 kDa
Excluded volume excluded_volume28866 ų
Envelope volume envelope_volume32980 ų
Hydration-shell volume shell_volume16000 ų
Envelope diameter envelope_diameter60.9
Shell Rg shell_rg23.22
Envelope Rg envelope_rg17.80
Shape Rg shape_rg17.65
Total Rg total_rg18.53
Total atoms total_atoms3148
Residues n_residues203
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 dmax59.2
Rg (real space) rg_real18.48
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real1.1230e+07
I(0) uncertainty (real space) i0_real_error1.5410e+05
Rg (reciprocal space) rg_reciprocal18.49
I(0) (reciprocal space) i0_reciprocal11230000.0000
Solution quality estimate total_estimate0.8143
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary21.9
Skewness Skewness skewness0.293
Kurtosis Kurtosis kurtosis-0.434
Angular range angular_range— – 0.4300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2152000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.862; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)