7ewm

Native crystal structure of S. cerevisiae Csn12 in complex with Thp3 and Sem1

Method: X-RAY DIFFRACTION Dmax: 112.2 Å Quality: GOOD

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

Protein THP3

Saccharomyces cerevisiae S288C

UniProt Q12049

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 A; UniProt 186–470 Not recorded Cop9 signalosome complex subunit 12 × 1 (P47130) 26S proteasome complex subunit SEM1 × 1 (O94742) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;12% PEG3350, 100 mM Sodium malonate buffer (pH 5.0) and 3% Methanol Resolution 2.90 Å R-free 0.251

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name THP3_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–289; UniProt 186–470

Cop9 signalosome complex subunit 12

Saccharomyces cerevisiae S288C

UniProt P47130

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 B; UniProt 1–423 Not recorded Protein THP3 × 1 (Q12049) 26S proteasome complex subunit SEM1 × 1 (O94742) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;12% PEG3350, 100 mM Sodium malonate buffer (pH 5.0) and 3% Methanol Resolution 2.90 Å R-free 0.251

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CSN12_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–423; UniProt 1–423

26S proteasome complex subunit SEM1

Saccharomyces cerevisiae S288C

UniProt O94742

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 C; UniProt 1–89 Not recorded Protein THP3 × 1 (Q12049) Cop9 signalosome complex subunit 12 × 1 (P47130) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;12% PEG3350, 100 mM Sodium malonate buffer (pH 5.0) and 3% Methanol Resolution 2.90 Å R-free 0.251

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.

35 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SEM1_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–89; UniProt 1–89

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 7ewm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7ewm
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7ewm
Deposition date deposition_date2021-05-25
Structure title titleNative crystal structure of S. cerevisiae Csn12 in complex with Thp3 and Sem1
Keywords keywordsComplex, Nucleic acid binding, Transcription, mRNA splicing; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.55
Radius of gyration Rg (electron density) rg_electron31.70
Forward intensity I(0) i0116020000.00
Molecular weight molecular_weight86809.0 kDa
Excluded volume excluded_volume109330 ų
Envelope volume envelope_volume145940 ų
Hydration-shell volume shell_volume38569 ų
Envelope diameter envelope_diameter117.6
Shell Rg shell_rg38.34
Envelope Rg envelope_rg31.88
Shape Rg shape_rg31.66
Total Rg total_rg32.41
Total atoms total_atoms6106
Residues n_residues739
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 dmax112.2
Rg (real space) rg_real32.50
Rg uncertainty (real space) rg_real_error0.83
I(0) (real space) i0_real1.1600e+08
I(0) uncertainty (real space) i0_real_error1.8430e+06
Rg (reciprocal space) rg_reciprocal32.53
I(0) (reciprocal space) i0_reciprocal116000000.0000
Solution quality estimate total_estimate0.8841
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.2
Skewness Skewness skewness0.252
Kurtosis Kurtosis kurtosis-0.449
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29370000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.848; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.971

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id7ewmA01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily990

8. Citations (1)

9. Files and Curves (10)