3kjl

Sgf11:Sus1 complex

Method: X-RAY DIFFRACTION Dmax: 115.4 Å Quality: REASONABLE

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;see publication, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.70 Å R-free 0.253
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;see publication, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.70 Å R-free 0.253
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;see publication, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.70 Å R-free 0.253
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;see publication, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.70 Å R-free 0.253

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 2–33 Fragment:Sus1-binding region Protein SUS1 × 1 (Q6WNK7) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;292 K;see publication, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.70 Å R-free 0.253
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 2–33 Fragment:Sus1-binding region Protein SUS1 × 1 (Q6WNK7) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;292 K;see publication, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.70 Å R-free 0.253
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 2–33 Fragment:Sus1-binding region Protein SUS1 × 1 (Q6WNK7) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;292 K;see publication, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.70 Å R-free 0.253
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 2–33 Fragment:Sus1-binding region Protein SUS1 × 1 (Q6WNK7) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;292 K;see publication, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.70 Å R-free 0.253

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 1–32; UniProt 2–33 Author chain F; PDBConstruct 1–32; UniProt 2–33 Author chain G; PDBConstruct 1–32; UniProt 2–33 Author chain H; PDBConstruct 1–32; UniProt 2–33

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 3kjl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3kjl
Deposition date deposition_date2009-11-03
Structure title titleSgf11:Sus1 complex
Keywords keywords;SAGA, Sus1, Sgf11, 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_guinier27.58
Radius of gyration Rg (electron density) rg_electron27.12
Forward intensity I(0) i043357800.00
Molecular weight molecular_weight51175.0 kDa
Excluded volume excluded_volume64370 ų
Envelope volume envelope_volume86311 ų
Hydration-shell volume shell_volume27986 ų
Envelope diameter envelope_diameter119.6
Shell Rg shell_rg32.29
Envelope Rg envelope_rg27.88
Shape Rg shape_rg27.12
Total Rg total_rg27.68
Total atoms total_atoms3593
Residues n_residues450
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 dmax115.4
Rg (real space) rg_real27.72
Rg uncertainty (real space) rg_real_error1.80
I(0) (real space) i0_real4.3360e+07
I(0) uncertainty (real space) i0_real_error8.6340e+05
Rg (reciprocal space) rg_reciprocal27.67
I(0) (reciprocal space) i0_reciprocal43360000.0000
Solution quality estimate total_estimate0.7454
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.8
Skewness Skewness skewness0.605
Kurtosis Kurtosis kurtosis0.592
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6657000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.310; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.759; Smooth: 0.997

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_idd3kjla_
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_idd3kjlb_
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_idd3kjlc_
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_idd3kjld_
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_id3kjlA00
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_id3kjlB00
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_id3kjlC00
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_id3kjlD00
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)