8yfe

Cryo EM structure of Komagataella phaffii Rat1-Rai1 complex

Method: ELECTRON MICROSCOPY Dmax: 155.7 Å Quality: GOOD

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

;5'-3' exoribonuclease ;

Komagataella phaffii

UniProt F2QV79

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 1–994 Chain C; UniProt 1–994 Mutation:D233A, D235A Decapping nuclease × 2 (F2QLF5) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;EMGP2 Resolution 3.47 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name F2QV79_KOMPC
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–994; UniProt 1–994 Author chain C; PDBConstruct 1–994; UniProt 1–994

Decapping nuclease

Komagataella phaffii

UniProt F2QLF5

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 1–381 Chain D; UniProt 1–381 Mutation:E213A, D215A,D233N ;5'-3' exoribonuclease ; × 2 (F2QV79) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;EMGP2 Resolution 3.47 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name F2QLF5_KOMPC
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–384; UniProt 1–381 Author chain D; PDBConstruct 4–384; UniProt 1–381

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 8yfe

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8yfe
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8yfe
Deposition date deposition_date2024-02-24
Structure title titleCryo EM structure of Komagataella phaffii Rat1-Rai1 complex
Keywords keywordstranscription termination, RNA polymerase II, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.99
Radius of gyration Rg (electron density) rg_electron48.48
Forward intensity I(0) i0834878000.00
Molecular weight molecular_weight245180.0 kDa
Excluded volume excluded_volume308960 ų
Envelope volume envelope_volume431040 ų
Hydration-shell volume shell_volume74504 ų
Envelope diameter envelope_diameter153.5
Shell Rg shell_rg51.62
Envelope Rg envelope_rg47.44
Shape Rg shape_rg48.46
Total Rg total_rg48.67
Total atoms total_atoms17315
Residues n_residues2107
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 dmax155.7
Rg (real space) rg_real48.86
Rg uncertainty (real space) rg_real_error1.12
I(0) (real space) i0_real8.3490e+08
I(0) uncertainty (real space) i0_real_error1.6180e+07
Rg (reciprocal space) rg_reciprocal48.99
I(0) (reciprocal space) i0_reciprocal835000000.0000
Solution quality estimate total_estimate0.8893
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary63.3
Skewness Skewness skewness0.154
Kurtosis Kurtosis kurtosis-0.703
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha151900000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.953; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.696

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)