9k1y

Structure of the SF3B core, harboring the R625H mutation in SF3B1, in complex with intron-U2 snRNA

Method: ELECTRON MICROSCOPY Dmax: 143.7 Å Quality: GOOD

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

Splicing factor 3B subunit 1

Homo sapiens

UniProt O75533

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 Heteromer Protein × 4 RNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain C; UniProt 453–1304 Mutation:R625H PHD finger-like domain-containing protein 5A × 1 (Q7RTV0) Splicing factor 3B subunit 3 × 1 (Q15393) Splicing factor 3B subunit 5 × 1 (Q9BWJ5) pre-mRNA intron × 1 U2 snRNA × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 Å

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.

71 other PDB entries and 77 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SF3B1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 46–897; UniProt 453–1304

PHD finger-like domain-containing protein 5A

Homo sapiens

UniProt Q7RTV0

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 Heteromer Protein × 4 RNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain D; UniProt 1–110 Not recorded Splicing factor 3B subunit 1 × 1 (O75533) Splicing factor 3B subunit 3 × 1 (Q15393) Splicing factor 3B subunit 5 × 1 (Q9BWJ5) pre-mRNA intron × 1 U2 snRNA × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 Å

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.

64 other PDB entries and 65 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PHF5A_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–110; UniProt 1–110

Splicing factor 3B subunit 3

Homo sapiens

UniProt Q15393

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 Heteromer Protein × 4 RNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain A; UniProt 1–1217 Not recorded Splicing factor 3B subunit 1 × 1 (O75533) PHD finger-like domain-containing protein 5A × 1 (Q7RTV0) Splicing factor 3B subunit 5 × 1 (Q9BWJ5) pre-mRNA intron × 1 U2 snRNA × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 Å

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.

66 other PDB entries and 66 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SF3B3_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 8–1224; UniProt 1–1217

Splicing factor 3B subunit 5

Homo sapiens

UniProt Q9BWJ5

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 Heteromer Protein × 4 RNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain B; UniProt 1–86 Not recorded Splicing factor 3B subunit 1 × 1 (O75533) PHD finger-like domain-containing protein 5A × 1 (Q7RTV0) Splicing factor 3B subunit 3 × 1 (Q15393) pre-mRNA intron × 1 U2 snRNA × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 Å

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.

66 other PDB entries and 66 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SF3B5_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 1–86; UniProt 1–86

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 9k1y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9k1y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9k1y
Deposition date deposition_date2024-10-16
最后修订 last_revision2025-09-03
Structure title titleStructure of the SF3B core, harboring the R625H mutation in SF3B1, in complex with intron-U2 snRNA
Keywords keywordsmRNA splicing, hotspot mutation, SPLICING/RNA, SPLICING-RNA complex; SPLICING/RNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.54
Radius of gyration Rg (electron density) rg_electron43.97
Forward intensity I(0) i0981537000.00
Molecular weight molecular_weight253380.0 kDa
Excluded volume excluded_volume314940 ų
Envelope volume envelope_volume447940 ų
Hydration-shell volume shell_volume82920 ų
Envelope diameter envelope_diameter149.1
Shell Rg shell_rg50.64
Envelope Rg envelope_rg43.18
Shape Rg shape_rg43.97
Total Rg total_rg44.28
Total atoms total_atoms17743
Residues n_residues2185
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 dmax143.7
Rg (real space) rg_real44.37
Rg uncertainty (real space) rg_real_error1.06
I(0) (real space) i0_real9.8150e+08
I(0) uncertainty (real space) i0_real_error1.8450e+07
Rg (reciprocal space) rg_reciprocal44.54
I(0) (reciprocal space) i0_reciprocal981700000.0000
Solution quality estimate total_estimate0.8957
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary53.4
Skewness Skewness skewness0.182
Kurtosis Kurtosis kurtosis-0.527
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha141100000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.917; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.892

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)