2m0g

Structure, phosphorylation and U2AF65 binding of the Nterminal Domain of splicing factor 1 during 3 splice site Recognition

Method: SOLUTION NMR Dmax: 62.7 Å Quality: REASONABLE

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

Splicing factor 1

Homo sapiens

UniProt Q15637

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–145 Fragment:UNP residues 1-145 Mutation:S137C Splicing factor U2AF 65 kDa subunit × 1 (P26368) SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Ionic strength (raw mmCIF value) 70;Pressure ambient NMR sample composition:100-600 uM [U-15N] protein, 100-600 uM [U-13C; U-15N] entity, 100-600 uM [U-13C; U-15N; U-2H] entity, 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.

8 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SF01_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–145; UniProt 1–145

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 372–475 Fragment:RRM 3 domain residues 372-475 Splicing factor 1 × 1 (Q15637) SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Ionic strength (raw mmCIF value) 70;Pressure ambient NMR sample composition:100-600 uM [U-15N] protein, 100-600 uM [U-13C; U-15N] entity, 100-600 uM [U-13C; U-15N; U-2H] entity, 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.

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
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–104; UniProt 372–475

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 2m0g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2m0g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2m0g
Deposition date deposition_date2012-10-25
Structure title titleStructure, phosphorylation and U2AF65 binding of the Nterminal Domain of splicing factor 1 during 3 splice site Recognition
Keywords keywordsspliceosome assembly, SF1, UHM, ULM, SPLICING; SPLICING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier23.25
Radius of gyration Rg (electron density) rg_electron22.95
Forward intensity I(0) i01204680000.00
Molecular weight molecular_weight286070.0 kDa
Excluded volume excluded_volume355940 ų
Envelope volume envelope_volume126290 ų
Hydration-shell volume shell_volume35469 ų
Envelope diameter envelope_diameter124.7
Shell Rg shell_rg36.49
Envelope Rg envelope_rg31.61
Shape Rg shape_rg22.93
Total Rg total_rg23.41
Total atoms total_atoms40040
Residues n_residues2490
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 dmax62.7
Rg (real space) rg_real21.85
Rg uncertainty (real space) rg_real_error0.11
I(0) (real space) i0_real1.1460e+09
I(0) uncertainty (real space) i0_real_error1.2180e+07
Rg (reciprocal space) rg_reciprocal23.45
I(0) (reciprocal space) i0_reciprocal1205000000.0000
Solution quality estimate total_estimate0.6827
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary25.1
Skewness Skewness skewness0.387
Kurtosis Kurtosis kurtosis-0.376
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha3.3170
Highest regularization parameter α highest_alpha2231000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.002; Oscil: 0.978; Stabil: 0.981; Sysdev: 0.000; Positv: 1.000; Valcen: 0.997; 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_idd2m0gb_
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.58.7.1 — Canonical RBD

CATH v4.4 (1 domains)

Domain ID domain_id2m0gB00
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)