3mhh

Structure of the SAGA Ubp8/Sgf11/Sus1/Sgf73 DUB module

Method: X-RAY DIFFRACTION Dmax: 94.1 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 Protein SUS1 × 1 (Q6WNK7) SAGA-associated factor 11 × 1 (Q03067) SAGA-associated factor 73 × 1 (P53165) ZN ZINC ION × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.2;293 K;0.1 M Na Citrate (5.2), 16% (w/v) PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.45 Å R-free 0.273

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 12 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

Protein 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 (Q03067) SAGA-associated factor 73 × 1 (P53165) ZN ZINC ION × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.2;293 K;0.1 M Na Citrate (5.2), 16% (w/v) PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.45 Å R-free 0.273

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 28 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

SAGA-associated factor 11

Saccharomyces cerevisiae

UniProt Q03067

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) Protein 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 5.2;293 K;0.1 M Na Citrate (5.2), 16% (w/v) PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.45 Å R-free 0.273

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.

10 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SGF11_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; 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 Fragment:residues 1-96 Ubiquitin carboxyl-terminal hydrolase 8 × 1 (P50102) Protein SUS1 × 1 (Q6WNK7) SAGA-associated factor 11 × 1 (Q03067) ZN ZINC ION × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.2;293 K;0.1 M Na Citrate (5.2), 16% (w/v) PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.45 Å R-free 0.273

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 17 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

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 3mhh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3mhh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3mhh
Deposition date deposition_date2010-04-08
Structure title titleStructure of the SAGA Ubp8/Sgf11/Sus1/Sgf73 DUB module
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_guinier28.74
Radius of gyration Rg (electron density) rg_electron27.47
Forward intensity I(0) i0111643000.00
Molecular weight molecular_weight81518.0 kDa
Excluded volume excluded_volume101240 ų
Envelope volume envelope_volume126500 ų
Hydration-shell volume shell_volume37546 ų
Envelope diameter envelope_diameter99.8
Shell Rg shell_rg35.45
Envelope Rg envelope_rg27.79
Shape Rg shape_rg27.43
Total Rg total_rg28.36
Total atoms total_atoms5689
Residues n_residues710
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 dmax94.1
Rg (real space) rg_real28.66
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real1.1160e+08
I(0) uncertainty (real space) i0_real_error1.5810e+06
Rg (reciprocal space) rg_reciprocal28.69
I(0) (reciprocal space) i0_reciprocal111600000.0000
Solution quality estimate total_estimate0.8903
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.2
Skewness Skewness skewness0.282
Kurtosis Kurtosis kurtosis-0.307
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15350000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.864; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.979

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3mhhb_
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 (5 domains)

Domain ID domain_id3mhhA01
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_id3mhhA02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology70 — Cathepsin B; Chain A
Homologous superfamily homologous superfamily10 — Cysteine proteinases
Domain ID domain_id3mhhB00
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_id3mhhC01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily210
Domain ID domain_id3mhhC02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology160 — Double Stranded RNA Binding Domain
Homologous superfamily homologous superfamily60 — Classic Zinc Finger

8. Citations (1)

9. Files and Curves (10)