← Back to search
2leb

Solution structure of human SRSF2 (SC35) RRM in complex with 5'-UCCAGU-3'

Method: SOLUTION NMR Dmax: 42.3 Å Quality: GOOD
▼

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

Serine/arginine-rich splicing factor 2

Homo sapiens

UniProt Q01130

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–RNA Monomer Protein × 1 RNA 1 PDB declaration: dimeric（2） Consistent with all polymer counts Chain A； UniProt 1–101 Fragment：RRM domain residues 1-101 ;RNA (5'-R(*UP*CP*CP*AP*GP*U)-3') ; × 1 SOLUTION NMR NMR measurement conditions：pH 5.5；310.8 K；Ionic strength (raw mmCIF value) 120；Pressure ambient NMR sample composition：0.75 mM [U-15N] SRSF2 RRM + UCCAGU1, 0.75 mM [U-13C; U-15N] SRSF2 RRM + UCCAGU2, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition：0.75 mM [U-15N] SRSF2 RRM + UCCAGU1, 100% D2O | 100% 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.

Other PDB Difference from Current Entry 2LEB Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2KN4 The structure of the RRM domain of SC35 Deposited 2009-08-14 Different construct Different oligomeric state Different experimental conditions Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 9–101（93 aa） Fragment：UNP residues 304-357 from P19909, UNP residues 9-101 from Q01130
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.8；305 K；Ionic strength (raw mmCIF value) 100；Pressure ambient
NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N] SC35-1, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N] SC35-2, 100% D2O | 100% D2O
NMR sample composition 0.5 mM [U-100% 15N] SC35-3, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM SC35-4, 100% D2O | 100% D2O
Resolution not provided
2LEA Solution structure of human SRSF2 (SC35) RRM Deposited 2011-06-15 Different oligomeric state Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–101（101 aa） Fragment：RRM domain residues 1-101
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.5；310.8 K；Ionic strength (raw mmCIF value) 120；Pressure ambient
NMR sample composition 0.75 mM [U-15N] SRSF2 RRM 1, 0.75 mM [U-13C; U-15N] SRSF2 RRM 2, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.75 mM [U-15N] SRSF2 RRM 1, 100% D2O | 100% D2O
Resolution not provided
2LEC Solution structure of human SRSF2 (SC35) RRM in complex with 5'-UGGAGU-3' Deposited 2011-06-15 Different experimental conditions Assembly 1 Protein–RNA Monomer；Protein × 1 PDB declaration: dimeric
Chain A 1–101（101 aa） Fragment：RRM domain residues 1-101
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.5；310.8 K；Ionic strength (raw mmCIF value) 120；Pressure ambient
NMR sample composition 0.75 mM [U-15N] SRSF2 RRM + UGGAGU1, 0.75 mM [U-13C; U-15N] SRSF2 RRM + UGGAGU2, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.75 mM [U-15N] SRSF2 RRM + UGGAGU1, 100% D2O | 100% D2O
Resolution not provided

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SRSF2_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 35–135； UniProt 1–101

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 2leb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2leb
Download Download
▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id2leb
Deposition date deposition_date2011-06-15
Structure title titleSolution structure of human SRSF2 (SC35) RRM in complex with 5'-UCCAGU-3'
Keywords keywordsSR protein, splicing factor, RNA protein complex, RNA binding protein-RNA complex; RNA binding protein/RNA
Experimental Method methodSOLUTION NMR
▼

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

Radius of gyration Rg (Guinier) rg_guinier14.00 Å
Radius of gyration Rg (electron density) rg_electron13.68 Å
Forward intensity I(0) i01356150000.00
Molecular weight molecular_weight270490.0 kDa
Excluded volume excluded_volume321090 ų
Envelope volume envelope_volume27972 ų
Hydration-shell volume shell_volume15197 ų
Envelope diameter envelope_diameter49.2 Å
Shell Rg shell_rg21.48 Å
Envelope Rg envelope_rg15.56 Å
Shape Rg shape_rg13.66 Å
Total Rg total_rg13.85 Å
Total atoms total_atoms35840
Residues n_residues2140
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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 dmax42.3 Å
Rg (real space) rg_real13.90 Å
Rg uncertainty (real space) rg_real_error0.21 Å
I(0) (real space) i0_real1.3560e+09
I(0) uncertainty (real space) i0_real_error1.3580e+07
Rg (reciprocal space) rg_reciprocal13.91 Å
I(0) (reciprocal space) i0_reciprocal1356000000.0000
Solution quality estimate total_estimate0.8286
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.8 Å
Skewness Skewness skewness0.106
Kurtosis Kurtosis kurtosis-0.429
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha403000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.000
▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (2)

▼

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2leba_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.7 — RNA-binding domain, RBD, aka RNA recognition motif (RRM)
Family Family familyd.58.7.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id2lebA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily330 — RRM (RNA recognition motif) domain
▶

8. Citations (1)

▶

9. Files and Curves (10)