6urg

Cryo-EM structure of human CPSF160-WDR33-CPSF30-CPSF100 PIM complex

Method: ELECTRON MICROSCOPY Dmax: 125.0 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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–1443 Not recorded ;pre-mRNA 3' end processing protein WDR33 ; × 1 (Q9C0J8) Cleavage and polyadenylation specificity factor subunit 4 × 1 (O95639) Cleavage and polyadenylation specificity factor subunit 2 × 1 (Q9P2I0) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;25 mM Tris-HCl, pH 8.0, 150 mM NaCl, 5 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–572 Not recorded Cleavage and polyadenylation specificity factor subunit 1 × 1 (Q10570) Cleavage and polyadenylation specificity factor subunit 4 × 1 (O95639) Cleavage and polyadenylation specificity factor subunit 2 × 1 (Q9P2I0) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;25 mM Tris-HCl, pH 8.0, 150 mM NaCl, 5 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 16–587; UniProt 1–572

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count 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) Cleavage and polyadenylation specificity factor subunit 2 × 1 (Q9P2I0) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;25 mM Tris-HCl, pH 8.0, 150 mM NaCl, 5 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 1–782 Not recorded Cleavage and polyadenylation specificity factor subunit 1 × 1 (Q10570) ;pre-mRNA 3' end processing protein WDR33 ; × 1 (Q9C0J8) Cleavage and polyadenylation specificity factor subunit 4 × 1 (O95639) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;25 mM Tris-HCl, pH 8.0, 150 mM NaCl, 5 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 4
Chains and sequence ranges Author chain F; PDBConstruct 1–782; UniProt 1–782

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 6urg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6urg
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6urg
Deposition date deposition_date2019-10-23
Structure title titleCryo-EM structure of human CPSF160-WDR33-CPSF30-CPSF100 PIM complex
Keywords keywords;pre-mRNA 3'-end processing, mammalin cleavage factor(mCF), CPSF100, mPSF, PROTEIN BINDING ;; PROTEIN BINDING
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.37
Radius of gyration Rg (electron density) rg_electron36.72
Forward intensity I(0) i0516120000.00
Molecular weight molecular_weight187750.0 kDa
Excluded volume excluded_volume236150 ų
Envelope volume envelope_volume297600 ų
Hydration-shell volume shell_volume65584 ų
Envelope diameter envelope_diameter127.7
Shell Rg shell_rg44.33
Envelope Rg envelope_rg36.67
Shape Rg shape_rg36.72
Total Rg total_rg37.21
Total atoms total_atoms13214
Residues n_residues1660
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 dmax125.0
Rg (real space) rg_real37.33
Rg uncertainty (real space) rg_real_error1.32
I(0) (real space) i0_real5.1610e+08
I(0) uncertainty (real space) i0_real_error9.9320e+06
Rg (reciprocal space) rg_reciprocal37.35
I(0) (reciprocal space) i0_reciprocal516100000.0000
Solution quality estimate total_estimate0.8666
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary44.6
Skewness Skewness skewness0.385
Kurtosis Kurtosis kurtosis-0.178
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha177500000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.810; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.837

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6urgA01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase

8. Citations (1)

9. Files and Curves (10)