3lru

hPRP8 Non-Native Subdomain

Method: X-RAY DIFFRACTION Dmax: 80.3 Å Quality: GOOD

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

Pre-mRNA-processing-splicing factor 8

Homo sapiens

UniProt Q6P2Q9

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 1831–1990 Chain B; UniProt 1831–1990 Fragment:UNP residues 1831-1990 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:vapour diffusion;pH 6;298 K;12% PEG4000, Tris Ph8, 1,3 diamino-propane, pH 6, vapour diffusion, temperature 298K Resolution 1.85 Å R-free 0.254

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.

100 other PDB entries and 112 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRP8_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–160; UniProt 1831–1990 Author chain B; PDBConstruct 1–160; UniProt 1831–1990

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 3lru

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3lru
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3lru
Deposition date deposition_date2010-02-11
Structure title titlehPRP8 Non-Native Subdomain
Keywords keywords;alternate folding of protein, Disease mutation, mRNA processing, mRNA splicing, Nucleus, Phosphoprotein, Retinitis pigmentosa, Ribonucleoprotein, RNA-binding, Sensory transduction, Spliceosome, Vision, RNA BINDING PROTEIN ;; RNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.40
Radius of gyration Rg (electron density) rg_electron23.77
Forward intensity I(0) i017852800.00
Molecular weight molecular_weight34562.0 kDa
Excluded volume excluded_volume44473 ų
Envelope volume envelope_volume55680 ų
Hydration-shell volume shell_volume20831 ų
Envelope diameter envelope_diameter81.4
Shell Rg shell_rg29.06
Envelope Rg envelope_rg23.87
Shape Rg shape_rg23.76
Total Rg total_rg24.57
Total atoms total_atoms2441
Residues n_residues300
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 dmax80.3
Rg (real space) rg_real24.54
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real1.7850e+07
I(0) uncertainty (real space) i0_real_error2.4480e+05
Rg (reciprocal space) rg_reciprocal24.51
I(0) (reciprocal space) i0_reciprocal17850000.0000
Solution quality estimate total_estimate0.8800
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.2
Skewness Skewness skewness0.447
Kurtosis Kurtosis kurtosis-0.397
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha3542000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.857; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.878; Smooth: 0.986

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)