3pbp

Structure of the yeast heterotrimeric Nup82-Nup159-Nup116 nucleoporin complex

Method: X-RAY DIFFRACTION Dmax: 188.9 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:N-terminal domain (NTD), UNP residues 1-452 Mutation:C396S Non-standard monomer:Yes (specific site not provided by mmCIF) Nucleoporin NUP116/NSP116 × 1 (Q02630) Nucleoporin NUP159 × 1 (P40477) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.6;298 K;PEG 400, sodium cacodylate, lithium sulfate, 2,5-hexanediol, pH 6.6, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.60 Å R-free 0.272
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 1–452 Fragment:N-terminal domain (NTD), UNP residues 1-452 Mutation:C396S Non-standard monomer:Yes (specific site not provided by mmCIF) Nucleoporin NUP116/NSP116 × 1 (Q02630) Nucleoporin NUP159 × 1 (P40477) PGE TRIETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.6;298 K;PEG 400, sodium cacodylate, lithium sulfate, 2,5-hexanediol, pH 6.6, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.60 Å R-free 0.272
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain G; UniProt 1–452 Fragment:N-terminal domain (NTD), UNP residues 1-452 Mutation:C396S Non-standard monomer:Yes (specific site not provided by mmCIF) Nucleoporin NUP116/NSP116 × 1 (Q02630) Nucleoporin NUP159 × 1 (P40477) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.6;298 K;PEG 400, sodium cacodylate, lithium sulfate, 2,5-hexanediol, pH 6.6, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.60 Å R-free 0.272
4 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain J; UniProt 1–452 Fragment:N-terminal domain (NTD), UNP residues 1-452 Mutation:C396S Non-standard monomer:Yes (specific site not provided by mmCIF) Nucleoporin NUP116/NSP116 × 1 (Q02630) Nucleoporin NUP159 × 1 (P40477) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.6;298 K;PEG 400, sodium cacodylate, lithium sulfate, 2,5-hexanediol, pH 6.6, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.60 Å R-free 0.272

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 6 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 Author chain J; PDBConstruct 1–452; UniProt 1–452

Nucleoporin NUP116/NSP116

Saccharomyces cerevisiae

UniProt Q02630

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 967–1113 Fragment:C-terminal domain (CTD), UNP residues 967-1113 Non-standard monomer:Yes (specific site not provided by mmCIF) Nucleoporin NUP82 × 1 (P40368) Nucleoporin NUP159 × 1 (P40477) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.6;298 K;PEG 400, sodium cacodylate, lithium sulfate, 2,5-hexanediol, pH 6.6, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.60 Å R-free 0.272
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 967–1113 Fragment:C-terminal domain (CTD), UNP residues 967-1113 Non-standard monomer:Yes (specific site not provided by mmCIF) Nucleoporin NUP82 × 1 (P40368) Nucleoporin NUP159 × 1 (P40477) PGE TRIETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.6;298 K;PEG 400, sodium cacodylate, lithium sulfate, 2,5-hexanediol, pH 6.6, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.60 Å R-free 0.272
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain H; UniProt 967–1113 Fragment:C-terminal domain (CTD), UNP residues 967-1113 Non-standard monomer:Yes (specific site not provided by mmCIF) Nucleoporin NUP82 × 1 (P40368) Nucleoporin NUP159 × 1 (P40477) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.6;298 K;PEG 400, sodium cacodylate, lithium sulfate, 2,5-hexanediol, pH 6.6, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.60 Å R-free 0.272
4 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain K; UniProt 967–1113 Fragment:C-terminal domain (CTD), UNP residues 967-1113 Non-standard monomer:Yes (specific site not provided by mmCIF) Nucleoporin NUP82 × 1 (P40368) Nucleoporin NUP159 × 1 (P40477) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.6;298 K;PEG 400, sodium cacodylate, lithium sulfate, 2,5-hexanediol, pH 6.6, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.60 Å R-free 0.272

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 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NU116_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–148; UniProt 967–1113 Author chain E; PDBConstruct 2–148; UniProt 967–1113 Author chain H; PDBConstruct 2–148; UniProt 967–1113 Author chain K; PDBConstruct 2–148; UniProt 967–1113

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 C; UniProt 1425–1460 Fragment:Tail, UNP residues 1425-1460 Non-standard monomer:Yes (specific site not provided by mmCIF) Nucleoporin NUP82 × 1 (P40368) Nucleoporin NUP116/NSP116 × 1 (Q02630) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.6;298 K;PEG 400, sodium cacodylate, lithium sulfate, 2,5-hexanediol, pH 6.6, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.60 Å R-free 0.272
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 1425–1460 Fragment:Tail, UNP residues 1425-1460 Non-standard monomer:Yes (specific site not provided by mmCIF) Nucleoporin NUP82 × 1 (P40368) Nucleoporin NUP116/NSP116 × 1 (Q02630) PGE TRIETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.6;298 K;PEG 400, sodium cacodylate, lithium sulfate, 2,5-hexanediol, pH 6.6, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.60 Å R-free 0.272
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain I; UniProt 1425–1460 Fragment:Tail, UNP residues 1425-1460 Non-standard monomer:Yes (specific site not provided by mmCIF) Nucleoporin NUP82 × 1 (P40368) Nucleoporin NUP116/NSP116 × 1 (Q02630) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.6;298 K;PEG 400, sodium cacodylate, lithium sulfate, 2,5-hexanediol, pH 6.6, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.60 Å R-free 0.272
4 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain L; UniProt 1425–1460 Fragment:Tail, UNP residues 1425-1460 Non-standard monomer:Yes (specific site not provided by mmCIF) Nucleoporin NUP82 × 1 (P40368) Nucleoporin NUP116/NSP116 × 1 (Q02630) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.6;298 K;PEG 400, sodium cacodylate, lithium sulfate, 2,5-hexanediol, pH 6.6, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.60 Å R-free 0.272

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 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NU159_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–36; UniProt 1425–1460 Author chain F; PDBConstruct 1–36; UniProt 1425–1460 Author chain I; PDBConstruct 1–36; UniProt 1425–1460 Author chain L; PDBConstruct 1–36; UniProt 1425–1460

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 3pbp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3pbp
Deposition date deposition_date2010-10-20
Structure title titleStructure of the yeast heterotrimeric Nup82-Nup159-Nup116 nucleoporin complex
Keywords keywords;beta-propeller, nucleoporin, mRNA export, mRNP remodelling, NUCLEOCYTOPLASMIC Transport, PROTEIN TRANSPORT, TRANSLOCATION, TRANSPORT, autoproteolysis, Fusion protein, PROTOONCOGENE, ONCOPROTEIN, Protein COMPLEX, Nucleus, Nuclear Envelope, Nuclear Pore Complex, TRANSPORT PROTEIN, STRUCTURAL PROTEIN ;; TRANSPORT PROTEIN,STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier57.20
Radius of gyration Rg (electron density) rg_electron57.18
Forward intensity I(0) i01071150000.00
Molecular weight molecular_weight280440.0 kDa
Excluded volume excluded_volume353060 ų
Envelope volume envelope_volume532390 ų
Hydration-shell volume shell_volume80302 ų
Envelope diameter envelope_diameter196.9
Shell Rg shell_rg56.23
Envelope Rg envelope_rg55.39
Shape Rg shape_rg57.21
Total Rg total_rg57.05
Total atoms total_atoms19653
Residues n_residues2401
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 dmax188.9
Rg (real space) rg_real57.22
Rg uncertainty (real space) rg_real_error1.83
I(0) (real space) i0_real1.0710e+09
I(0) uncertainty (real space) i0_real_error2.1000e+07
Rg (reciprocal space) rg_reciprocal57.15
I(0) (reciprocal space) i0_reciprocal1071000000.0000
Solution quality estimate total_estimate0.8766
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary77.0
Skewness Skewness skewness0.223
Kurtosis Kurtosis kurtosis-0.545
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha62110000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.917; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.667

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id3pbpB00
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_id3pbpE00
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_id3pbpH00
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_id3pbpK00
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)