9ngo

CRYO-EM STRUCTURE OF HUMAN U7 SNRNP WITH METHYLATED noncleavable H2A* SUBSTRATE PRE-MRNA (FOCUS MAP)

Method: ELECTRON MICROSCOPY Dmax: 111.0 Å Quality: GOOD

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

Cleavage and polyadenylation specificity factor subunit 3

Homo sapiens

UniProt Q9UKF6

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain H; UniProt 1–684 Not recorded Cleavage and polyadenylation specificity factor subunit 2 × 1 (Q9P2I0) Symplekin × 1 (Q92797) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.01 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.

9 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CPSF3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain H; PDBConstruct 1–684; UniProt 1–684

Cleavage and polyadenylation specificity factor subunit 2

Homo sapiens

UniProt Q9P2I0

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain I; UniProt 1–782 Not recorded Cleavage and polyadenylation specificity factor subunit 3 × 1 (Q9UKF6) Symplekin × 1 (Q92797) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.01 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CPSF2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain I; PDBConstruct 1–782; UniProt 1–782

Symplekin

Homo sapiens

UniProt Q92797

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain J; UniProt 30–1101 Not recorded Cleavage and polyadenylation specificity factor subunit 3 × 1 (Q9UKF6) Cleavage and polyadenylation specificity factor subunit 2 × 1 (Q9P2I0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.01 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 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SYMPK_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain J; PDBConstruct 1–1072; UniProt 30–1101

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 9ngo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9ngo
Deposition date deposition_date2025-02-22
Structure title titleCRYO-EM STRUCTURE OF HUMAN U7 SNRNP WITH METHYLATED noncleavable H2A* SUBSTRATE PRE-MRNA (FOCUS MAP)
Keywords keywords;Methylated RNA, 3' end processing, U7 snRNP, Histone pre-mRNA, RNA BINDING PROTEIN ;; RNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier30.85
Radius of gyration Rg (electron density) rg_electron30.54
Forward intensity I(0) i058407600.00
Molecular weight molecular_weight61724.0 kDa
Excluded volume excluded_volume78252 ų
Envelope volume envelope_volume107000 ų
Hydration-shell volume shell_volume30468 ų
Envelope diameter envelope_diameter117.3
Shell Rg shell_rg35.61
Envelope Rg envelope_rg30.97
Shape Rg shape_rg30.53
Total Rg total_rg31.11
Total atoms total_atoms4334
Residues n_residues546
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 dmax111.0
Rg (real space) rg_real31.00
Rg uncertainty (real space) rg_real_error1.13
I(0) (real space) i0_real5.8410e+07
I(0) uncertainty (real space) i0_real_error8.8260e+05
Rg (reciprocal space) rg_reciprocal30.94
I(0) (reciprocal space) i0_reciprocal58400000.0000
Solution quality estimate total_estimate0.8416
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.6
Skewness Skewness skewness0.483
Kurtosis Kurtosis kurtosis-0.066
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17570000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.751; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.759; Smooth: 0.925

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)