6fuw

Cryo-EM structure of the human CPSF160-WDR33-CPSF30 complex bound to the PAS AAUAAA motif at 3.1 Angstrom resolution

Method: ELECTRON MICROSCOPY Dmax: 130.8 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) Cleavage and polyadenylation specificity factor subunit 4 × 1 (O95639) ;RNA (5'-R(P*AP*AP*UP*AP*AP*AP*GP*G)-3') ; × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;15 seconds wait time prior to blotting Resolution 3.07 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 4–1446; 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 1–410 Not recorded Cleavage and polyadenylation specificity factor subunit 1 × 1 (Q10570) Cleavage and polyadenylation specificity factor subunit 4 × 1 (O95639) ;RNA (5'-R(P*AP*AP*UP*AP*AP*AP*GP*G)-3') ; × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;15 seconds wait time prior to blotting Resolution 3.07 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 4–413; UniProt 1–410

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 1–178 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*AP*UP*AP*AP*AP*GP*G)-3') ; × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;15 seconds wait time prior to blotting Resolution 3.07 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 O95639-3
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–178; UniProt 1–178

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 6fuw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6fuw
Deposition date deposition_date2018-02-28
Structure title titleCryo-EM structure of the human CPSF160-WDR33-CPSF30 complex bound to the PAS AAUAAA motif at 3.1 Angstrom resolution
Keywords keywords;3' pre-mRNA processing, polyadenylation, CPSF, beta propeller, AAUAAA, 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_guinier38.60
Radius of gyration Rg (electron density) rg_electron37.97
Forward intensity I(0) i0545046000.00
Molecular weight molecular_weight191040.0 kDa
Excluded volume excluded_volume239310 ų
Envelope volume envelope_volume311040 ų
Hydration-shell volume shell_volume66776 ų
Envelope diameter envelope_diameter132.8
Shell Rg shell_rg45.06
Envelope Rg envelope_rg37.89
Shape Rg shape_rg37.95
Total Rg total_rg38.45
Total atoms total_atoms13421
Residues n_residues1672
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 dmax130.8
Rg (real space) rg_real38.59
Rg uncertainty (real space) rg_real_error1.02
I(0) (real space) i0_real5.4500e+08
I(0) uncertainty (real space) i0_real_error1.0180e+07
Rg (reciprocal space) rg_reciprocal38.60
I(0) (reciprocal space) i0_reciprocal545100000.0000
Solution quality estimate total_estimate0.8686
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.7
Skewness Skewness skewness0.393
Kurtosis Kurtosis kurtosis-0.222
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha134900000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.799; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.891

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_id6fuwA01
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)