9oxe

CRYO-EM STRUCTURE OF the human mPSF IN COMPLEX WITH THE AGUAAA poly(A) signal

Method: ELECTRON MICROSCOPY Dmax: 128.2 Å Quality: GOOD

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

Cleavage and polyadenylation specificity factor subunit 1

Homo sapiens

UniProt Q10570

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 × 3 RNA 1 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 1–1443 Not recorded ;pre-mRNA 3' end processing protein WDR33 ; × 1 (Q9C0J8) Isoform 2 of Cleavage and polyadenylation specificity factor subunit 4 × 1 (O95639) ;RNA (5'-R(P*AP*GP*UP*AP*AP*AP*C)-3') ; × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.53 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CPSF1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1443; UniProt 1–1443

;pre-mRNA 3' end processing protein WDR33 ;

Homo sapiens

UniProt Q9C0J8

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 × 3 RNA 1 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain B; UniProt 2–572 Not recorded Cleavage and polyadenylation specificity factor subunit 1 × 1 (Q10570) Isoform 2 of Cleavage and polyadenylation specificity factor subunit 4 × 1 (O95639) ;RNA (5'-R(P*AP*GP*UP*AP*AP*AP*C)-3') ; × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.53 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WDR33_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–574; UniProt 2–572

Isoform 2 of Cleavage and polyadenylation specificity factor subunit 4

Homo sapiens

UniProt O95639

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 × 3 RNA 1 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain C; UniProt 1–244 Not recorded Cleavage and polyadenylation specificity factor subunit 1 × 1 (Q10570) ;pre-mRNA 3' end processing protein WDR33 ; × 1 (Q9C0J8) ;RNA (5'-R(P*AP*GP*UP*AP*AP*AP*C)-3') ; × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.53 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.

11 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CPSF4_HUMAN
Isoform O95639-2
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–244; UniProt 1–244

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 9oxe

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9oxe
Deposition date deposition_date2025-06-03
Structure title titleCRYO-EM STRUCTURE OF the human mPSF IN COMPLEX WITH THE AGUAAA poly(A) signal
Keywords keywordspolyadenylation signal, RNA BINDING PROTEIN, RNA BINDING PROTEIN-RNA complex; RNA BINDING PROTEIN/RNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.87
Radius of gyration Rg (electron density) rg_electron37.27
Forward intensity I(0) i0537433000.00
Molecular weight molecular_weight190150.0 kDa
Excluded volume excluded_volume238410 ų
Envelope volume envelope_volume297070 ų
Hydration-shell volume shell_volume64980 ų
Envelope diameter envelope_diameter126.9
Shell Rg shell_rg44.43
Envelope Rg envelope_rg37.11
Shape Rg shape_rg37.25
Total Rg total_rg37.75
Total atoms total_atoms13359
Residues n_residues1667
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 dmax128.2
Rg (real space) rg_real37.84
Rg uncertainty (real space) rg_real_error1.22
I(0) (real space) i0_real5.3740e+08
I(0) uncertainty (real space) i0_real_error9.2940e+06
Rg (reciprocal space) rg_reciprocal37.86
I(0) (reciprocal space) i0_reciprocal537400000.0000
Solution quality estimate total_estimate0.8714
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.8
Skewness Skewness skewness0.379
Kurtosis Kurtosis kurtosis-0.237
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha129900000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.803; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.916

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)