3tkn

Structure of the Nup82-Nup159-Nup98 heterotrimer

Method: X-RAY DIFFRACTION Dmax: 138.0 Å Quality: GOOD

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

Nucleoporin NUP82

Saccharomyces cerevisiae

UniProt P40368

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–452 Fragment:UNP residues 1-452 Nucleoporin NUP159 × 1 (P40477) Nucleoporin 98 × 1 (Q6PFD9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;18.5% PEG3350, 100 mM potassium thiocyanate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K Resolution 3.40 Å R-free 0.285
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 1–452 Fragment:UNP residues 1-452 Nucleoporin NUP159 × 1 (P40477) Nucleoporin 98 × 1 (Q6PFD9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;18.5% PEG3350, 100 mM potassium thiocyanate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K Resolution 3.40 Å R-free 0.285
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain G; UniProt 1–452 Fragment:UNP residues 1-452 Nucleoporin NUP159 × 1 (P40477) Nucleoporin 98 × 1 (Q6PFD9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;18.5% PEG3350, 100 mM potassium thiocyanate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K Resolution 3.40 Å R-free 0.285

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.

2 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NUP82_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–452; UniProt 1–452 Author chain D; PDBConstruct 1–452; UniProt 1–452 Author chain G; PDBConstruct 1–452; UniProt 1–452

Nucleoporin NUP159

Saccharomyces cerevisiae

UniProt P40477

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1425–1460 Fragment:UNP residues 1425-1460 Nucleoporin NUP82 × 1 (P40368) Nucleoporin 98 × 1 (Q6PFD9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;18.5% PEG3350, 100 mM potassium thiocyanate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K Resolution 3.40 Å R-free 0.285
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 1425–1460 Fragment:UNP residues 1425-1460 Nucleoporin NUP82 × 1 (P40368) Nucleoporin 98 × 1 (Q6PFD9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;18.5% PEG3350, 100 mM potassium thiocyanate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K Resolution 3.40 Å R-free 0.285
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain H; UniProt 1425–1460 Fragment:UNP residues 1425-1460 Nucleoporin NUP82 × 1 (P40368) Nucleoporin 98 × 1 (Q6PFD9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;18.5% PEG3350, 100 mM potassium thiocyanate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K Resolution 3.40 Å R-free 0.285

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.

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

View Construct and Data Evidence
UniProt name NU159_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–39; UniProt 1425–1460 Author chain E; PDBConstruct 4–39; UniProt 1425–1460 Author chain H; PDBConstruct 4–39; UniProt 1425–1460

Nucleoporin 98

Mus musculus

UniProt Q6PFD9

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 732–880 Fragment:UNP residues 732-880 Nucleoporin NUP82 × 1 (P40368) Nucleoporin NUP159 × 1 (P40477) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;18.5% PEG3350, 100 mM potassium thiocyanate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K Resolution 3.40 Å R-free 0.285
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 732–880 Fragment:UNP residues 732-880 Nucleoporin NUP82 × 1 (P40368) Nucleoporin NUP159 × 1 (P40477) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;18.5% PEG3350, 100 mM potassium thiocyanate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K Resolution 3.40 Å R-free 0.285
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain I; UniProt 732–880 Fragment:UNP residues 732-880 Nucleoporin NUP82 × 1 (P40368) Nucleoporin NUP159 × 1 (P40477) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;18.5% PEG3350, 100 mM potassium thiocyanate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K Resolution 3.40 Å R-free 0.285

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 Q6PFD9_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 4–152; UniProt 732–880 Author chain F; PDBConstruct 4–152; UniProt 732–880 Author chain I; PDBConstruct 4–152; UniProt 732–880

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 3tkn

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3tkn
Deposition date deposition_date2011-08-28
Structure title titleStructure of the Nup82-Nup159-Nup98 heterotrimer
Keywords keywordsprotein complex, oncoprotein, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier44.16
Radius of gyration Rg (electron density) rg_electron43.36
Forward intensity I(0) i0631449000.00
Molecular weight molecular_weight213000.0 kDa
Excluded volume excluded_volume268890 ų
Envelope volume envelope_volume370840 ų
Hydration-shell volume shell_volume70499 ų
Envelope diameter envelope_diameter142.6
Shell Rg shell_rg49.49
Envelope Rg envelope_rg42.59
Shape Rg shape_rg43.39
Total Rg total_rg43.54
Total atoms total_atoms15021
Residues n_residues1870
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 dmax138.0
Rg (real space) rg_real43.98
Rg uncertainty (real space) rg_real_error0.88
I(0) (real space) i0_real6.3140e+08
I(0) uncertainty (real space) i0_real_error1.1120e+07
Rg (reciprocal space) rg_reciprocal44.16
I(0) (reciprocal space) i0_reciprocal631600000.0000
Solution quality estimate total_estimate0.8975
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary61.3
Skewness Skewness skewness0.124
Kurtosis Kurtosis kurtosis-0.597
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha94960000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.954; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.807

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id3tknC00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1610 — c-terminal autoproteolytic domain of nucleoporin nup98
Homologous superfamily homologous superfamily10 — Peptidase S59, nucleoporin
Domain ID domain_id3tknF00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1610 — c-terminal autoproteolytic domain of nucleoporin nup98
Homologous superfamily homologous superfamily10 — Peptidase S59, nucleoporin
Domain ID domain_id3tknI00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1610 — c-terminal autoproteolytic domain of nucleoporin nup98
Homologous superfamily homologous superfamily10 — Peptidase S59, nucleoporin

8. Citations (1)

9. Files and Curves (10)