6xaw

Crystal Structure Analysis of SIN3-UME6

Method: X-RAY DIFFRACTION Dmax: 41.5 Å Quality: GOOD

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

Transcriptional regulatory protein SIN3

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P22579

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 402–473 Not recorded Transcriptional regulatory protein UME6 × 1 (P39001) BR BROMIDE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.8;293 K;100mM Tris, pH 8.8, 1.36M sodium citrate Resolution 1.84 Å R-free 0.212

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.

28 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SIN3_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–76; UniProt 402–473

Transcriptional regulatory protein UME6

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P39001

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 500–543 Not recorded Transcriptional regulatory protein SIN3 × 1 (P22579) BR BROMIDE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.8;293 K;100mM Tris, pH 8.8, 1.36M sodium citrate Resolution 1.84 Å R-free 0.212

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name UME6_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–46; UniProt 500–543

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 6xaw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6xaw
Deposition date deposition_date2020-06-04
Structure title titleCrystal Structure Analysis of SIN3-UME6
Keywords keywordsRPD3 histone deacetylase complexes, pigenetic repression, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier13.73
Radius of gyration Rg (electron density) rg_electron12.00
Forward intensity I(0) i02034000.00
Molecular weight molecular_weight9899.0 kDa
Excluded volume excluded_volume12481 ų
Envelope volume envelope_volume13746 ų
Hydration-shell volume shell_volume9834 ų
Envelope diameter envelope_diameter39.9
Shell Rg shell_rg17.67
Envelope Rg envelope_rg12.33
Shape Rg shape_rg11.98
Total Rg total_rg13.49
Total atoms total_atoms701
Residues n_residues85
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 dmax41.5
Rg (real space) rg_real13.61
Rg uncertainty (real space) rg_real_error0.19
I(0) (real space) i0_real2.0340e+06
I(0) uncertainty (real space) i0_real_error2.1060e+04
Rg (reciprocal space) rg_reciprocal13.62
I(0) (reciprocal space) i0_reciprocal2034000.0000
Solution quality estimate total_estimate0.8922
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.9
Skewness Skewness skewness0.008
Kurtosis Kurtosis kurtosis-0.337
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha463100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.879; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.968; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd6xawa_
Class classa — All alpha proteins
Fold Fold folda.59 — PAH2 domain
Superfamily Superfamily superfamilya.59.1 — PAH2 domain
Family Family familya.59.1.1 — PAH2 domain

8. Citations (1)

9. Files and Curves (10)