3kik

Sgf11:Sus1 complex

Method: X-RAY DIFFRACTION Dmax: 96.1 Å Quality: GOOD

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

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–96 Not recorded SAGA-associated factor 11 × 1 (Q03067) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;292 K;3.2 M Na formate. See publication for details, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.10 Å R-free 0.231
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–96 Not recorded SAGA-associated factor 11 × 1 (Q03067) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;292 K;3.2 M Na formate. See publication for details, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.10 Å R-free 0.231
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–96 Not recorded SAGA-associated factor 11 × 1 (Q03067) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;292 K;3.2 M Na formate. See publication for details, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.10 Å R-free 0.231
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–96 Not recorded SAGA-associated factor 11 × 1 (Q03067) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;292 K;3.2 M Na formate. See publication for details, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.10 Å R-free 0.231

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 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SUS1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–96; UniProt 1–96 Author chain B; PDBConstruct 1–96; UniProt 1–96 Author chain C; PDBConstruct 1–96; UniProt 1–96 Author chain D; 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 7–33 Fragment:Sus1 binding region of Sgf11 Protein SUS1 × 1 (Q6WNK7) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;292 K;3.2 M Na formate. See publication for details, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.10 Å R-free 0.231
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 7–33 Fragment:Sus1 binding region of Sgf11 Protein SUS1 × 1 (Q6WNK7) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;292 K;3.2 M Na formate. See publication for details, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.10 Å R-free 0.231
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 7–33 Fragment:Sus1 binding region of Sgf11 Protein SUS1 × 1 (Q6WNK7) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;292 K;3.2 M Na formate. See publication for details, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.10 Å R-free 0.231
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 7–33 Fragment:Sus1 binding region of Sgf11 Protein SUS1 × 1 (Q6WNK7) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;292 K;3.2 M Na formate. See publication for details, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.10 Å R-free 0.231

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 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SGF11_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 3–29; UniProt 7–33 Author chain F; PDBConstruct 3–29; UniProt 7–33 Author chain G; PDBConstruct 3–29; UniProt 7–33 Author chain H; PDBConstruct 3–29; UniProt 7–33

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 3kik

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3kik
Deposition date deposition_date2009-11-02
Structure title titleSgf11:Sus1 complex
Keywords keywords;articulated hirpin fold, SAGA complex, Activator, Chromatin regulator, Metal-binding, Nucleus, Transcription, Transcription regulation, Zinc, Zinc-finger, mRNA transport, Nuclear pore complex, Protein transport, Translocation, Transport ;; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.92
Radius of gyration Rg (electron density) rg_electron28.19
Forward intensity I(0) i049065200.00
Molecular weight molecular_weight54377.0 kDa
Excluded volume excluded_volume68115 ų
Envelope volume envelope_volume90554 ų
Hydration-shell volume shell_volume27914 ų
Envelope diameter envelope_diameter101.0
Shell Rg shell_rg34.20
Envelope Rg envelope_rg28.02
Shape Rg shape_rg28.16
Total Rg total_rg28.90
Total atoms total_atoms3814
Residues n_residues481
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 dmax96.1
Rg (real space) rg_real28.99
Rg uncertainty (real space) rg_real_error0.90
I(0) (real space) i0_real4.9070e+07
I(0) uncertainty (real space) i0_real_error7.5400e+05
Rg (reciprocal space) rg_reciprocal28.96
I(0) (reciprocal space) i0_reciprocal49060000.0000
Solution quality estimate total_estimate0.8825
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.2
Skewness Skewness skewness0.396
Kurtosis Kurtosis kurtosis-0.342
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6383000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.885; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.931; Smooth: 0.883

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd3kika_
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_idd3kikb_
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_idd3kikc_
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_idd3kikd_
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 (4 domains)

Domain ID domain_id3kikA00
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_id3kikB00
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_id3kikC00
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_id3kikD00
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)