4wa6

Structure of yeast SAGA DUBm with Sgf73 N59D mutant at 2.36 angstroms resolution

Method: X-RAY DIFFRACTION Dmax: 148.2 Å Quality: GOOD

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

Ubiquitin carboxyl-terminal hydrolase 8

Saccharomyces cerevisiae

UniProt P50102

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 1–471 Not recorded Transcription and mRNA export factor SUS1 × 1 (Q6WNK7) SAGA-associated factor 11 × 1 (A6ZWK1) SAGA-associated factor 73 × 1 (P53165) ZN ZINC ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;100mM Bis Tris, 18% PEG3350, 100mM Ammonium Sulfate Resolution 2.36 Å R-free 0.244
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–471 Not recorded Transcription and mRNA export factor SUS1 × 1 (Q6WNK7) SAGA-associated factor 11 × 1 (A6ZWK1) SAGA-associated factor 73 × 1 (P53165) ZN ZINC ION × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;100mM Bis Tris, 18% PEG3350, 100mM Ammonium Sulfate Resolution 2.36 Å R-free 0.244
3 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–471 Chain D; UniProt 1–471 Not recorded Transcription and mRNA export factor SUS1 × 2 (Q6WNK7) SAGA-associated factor 11 × 2 (A6ZWK1) SAGA-associated factor 73 × 2 (P53165) ZN ZINC ION × 15 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;100mM Bis Tris, 18% PEG3350, 100mM Ammonium Sulfate Resolution 2.36 Å R-free 0.244

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.

9 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBP8_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–476; UniProt 1–471 Author chain D; PDBConstruct 6–476; UniProt 1–471

Transcription and mRNA export factor SUS1

Saccharomyces cerevisiae

UniProt Q6WNK7

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 1–96 Not recorded Ubiquitin carboxyl-terminal hydrolase 8 × 1 (P50102) SAGA-associated factor 11 × 1 (A6ZWK1) SAGA-associated factor 73 × 1 (P53165) ZN ZINC ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;100mM Bis Tris, 18% PEG3350, 100mM Ammonium Sulfate Resolution 2.36 Å R-free 0.244
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 1–96 Not recorded Ubiquitin carboxyl-terminal hydrolase 8 × 1 (P50102) SAGA-associated factor 11 × 1 (A6ZWK1) SAGA-associated factor 73 × 1 (P53165) ZN ZINC ION × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;100mM Bis Tris, 18% PEG3350, 100mM Ammonium Sulfate Resolution 2.36 Å R-free 0.244
3 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 1–96 Chain F; UniProt 1–96 Not recorded Ubiquitin carboxyl-terminal hydrolase 8 × 2 (P50102) SAGA-associated factor 11 × 2 (A6ZWK1) SAGA-associated factor 73 × 2 (P53165) ZN ZINC ION × 15 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;100mM Bis Tris, 18% PEG3350, 100mM Ammonium Sulfate Resolution 2.36 Å R-free 0.244

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.

15 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SUS1_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–96; UniProt 1–96 Author chain F; PDBConstruct 1–96; UniProt 1–96

SAGA-associated factor 11

Saccharomyces cerevisiae

UniProt A6ZWK1

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 1–99 Not recorded Ubiquitin carboxyl-terminal hydrolase 8 × 1 (P50102) Transcription and mRNA export factor SUS1 × 1 (Q6WNK7) SAGA-associated factor 73 × 1 (P53165) ZN ZINC ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;100mM Bis Tris, 18% PEG3350, 100mM Ammonium Sulfate Resolution 2.36 Å R-free 0.244
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain G; UniProt 1–99 Not recorded Ubiquitin carboxyl-terminal hydrolase 8 × 1 (P50102) Transcription and mRNA export factor SUS1 × 1 (Q6WNK7) SAGA-associated factor 73 × 1 (P53165) ZN ZINC ION × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;100mM Bis Tris, 18% PEG3350, 100mM Ammonium Sulfate Resolution 2.36 Å R-free 0.244
3 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain C; UniProt 1–99 Chain G; UniProt 1–99 Not recorded Ubiquitin carboxyl-terminal hydrolase 8 × 2 (P50102) Transcription and mRNA export factor SUS1 × 2 (Q6WNK7) SAGA-associated factor 73 × 2 (P53165) ZN ZINC ION × 15 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;100mM Bis Tris, 18% PEG3350, 100mM Ammonium Sulfate Resolution 2.36 Å R-free 0.244

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 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SGF11_YEAS7
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–99; UniProt 1–99 Author chain G; PDBConstruct 1–99; UniProt 1–99

SAGA-associated factor 73

Saccharomyces cerevisiae

UniProt P53165

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 E; UniProt 1–96 Mutation:N59D Ubiquitin carboxyl-terminal hydrolase 8 × 1 (P50102) Transcription and mRNA export factor SUS1 × 1 (Q6WNK7) SAGA-associated factor 11 × 1 (A6ZWK1) ZN ZINC ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;100mM Bis Tris, 18% PEG3350, 100mM Ammonium Sulfate Resolution 2.36 Å R-free 0.244
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain H; UniProt 1–96 Mutation:N59D Ubiquitin carboxyl-terminal hydrolase 8 × 1 (P50102) Transcription and mRNA export factor SUS1 × 1 (Q6WNK7) SAGA-associated factor 11 × 1 (A6ZWK1) ZN ZINC ION × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;100mM Bis Tris, 18% PEG3350, 100mM Ammonium Sulfate Resolution 2.36 Å R-free 0.244
3 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 1–96 Chain H; UniProt 1–96 Mutation:N59D Ubiquitin carboxyl-terminal hydrolase 8 × 2 (P50102) Transcription and mRNA export factor SUS1 × 2 (Q6WNK7) SAGA-associated factor 11 × 2 (A6ZWK1) ZN ZINC ION × 15 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;100mM Bis Tris, 18% PEG3350, 100mM Ammonium Sulfate Resolution 2.36 Å R-free 0.244

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.

13 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SGF73_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 1–96; UniProt 1–96 Author chain H; PDBConstruct 1–96; UniProt 1–96

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 4wa6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4wa6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4wa6
Deposition date deposition_date2014-08-28
Structure title titleStructure of yeast SAGA DUBm with Sgf73 N59D mutant at 2.36 angstroms resolution
Keywords keywordsMulti-Protein Complex, Hydrolase-transcription complex; hydrolase/transcription
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier43.60
Radius of gyration Rg (electron density) rg_electron43.43
Forward intensity I(0) i0377529000.00
Molecular weight molecular_weight157060.0 kDa
Excluded volume excluded_volume195540 ų
Envelope volume envelope_volume265710 ų
Hydration-shell volume shell_volume52725 ų
Envelope diameter envelope_diameter159.6
Shell Rg shell_rg45.84
Envelope Rg envelope_rg43.34
Shape Rg shape_rg43.37
Total Rg total_rg43.75
Total atoms total_atoms10950
Residues n_residues1364
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 dmax148.2
Rg (real space) rg_real43.92
Rg uncertainty (real space) rg_real_error1.77
I(0) (real space) i0_real3.7750e+08
I(0) uncertainty (real space) i0_real_error7.3740e+06
Rg (reciprocal space) rg_reciprocal43.61
I(0) (reciprocal space) i0_reciprocal377400000.0000
Solution quality estimate total_estimate0.8316
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary37.0
Skewness Skewness skewness0.482
Kurtosis Kurtosis kurtosis-0.458
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha66250000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.775; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.831; Smooth: 0.652

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4wa6b_
Class classa — All alpha proteins
Fold Fold folda.301 — Sus1-like
Superfamily Superfamily superfamilya.301.1 — Sus1-like
Family Family familya.301.1.1 — Sus1-like
Domain ID domain_idd4wa6f_
Class classa — All alpha proteins
Fold Fold folda.301 — Sus1-like
Superfamily Superfamily superfamilya.301.1 — Sus1-like
Family Family familya.301.1.1 — Sus1-like

CATH v4.4 (6 domains)

Domain ID domain_id4wa6A01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology40 — Herpes Virus-1
Homologous superfamily homologous superfamily10 — Zinc/RING finger domain, C3HC4 (zinc finger)
Domain ID domain_id4wa6A02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology70 — Cathepsin B; Chain A
Homologous superfamily homologous superfamily10 — Cysteine proteinases
Domain ID domain_id4wa6B00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology246 — Serum Albumin; Chain A, Domain 1
Homologous superfamily homologous superfamily140 — ENY2/SUS1
Domain ID domain_id4wa6D01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology40 — Herpes Virus-1
Homologous superfamily homologous superfamily10 — Zinc/RING finger domain, C3HC4 (zinc finger)
Domain ID domain_id4wa6D02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology70 — Cathepsin B; Chain A
Homologous superfamily homologous superfamily10 — Cysteine proteinases
Domain ID domain_id4wa6F00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology246 — Serum Albumin; Chain A, Domain 1
Homologous superfamily homologous superfamily140 — ENY2/SUS1

8. Citations (1)

9. Files and Curves (10)