3ewe

Crystal Structure of the Nup85/Seh1 Complex

Method: X-RAY DIFFRACTION Dmax: 146.7 Å Quality: GOOD

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

Nucleoporin SEH1

Saccharomyces cerevisiae

UniProt P53011

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 1–349 Not recorded Nucleoporin NUP85 × 1 (P46673) X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;289 K;18% PEG 3350, 0.1M Bis Tris propane, 0.2M Sodium Citrate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 3.50 Å R-free 0.369
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–349 Not recorded Nucleoporin NUP85 × 1 (P46673) X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;289 K;18% PEG 3350, 0.1M Bis Tris propane, 0.2M Sodium Citrate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 3.50 Å R-free 0.369
3 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–349 Chain C; UniProt 1–349 Not recorded Nucleoporin NUP85 × 2 (P46673) X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;289 K;18% PEG 3350, 0.1M Bis Tris propane, 0.2M Sodium Citrate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 3.50 Å R-free 0.369

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 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SEH1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–349; UniProt 1–349 Author chain C; PDBConstruct 1–349; UniProt 1–349

Nucleoporin NUP85

Saccharomyces cerevisiae

UniProt P46673

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 B; UniProt 1–564 Fragment:UNP residues 1-564 Nucleoporin SEH1 × 1 (P53011) X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;289 K;18% PEG 3350, 0.1M Bis Tris propane, 0.2M Sodium Citrate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 3.50 Å R-free 0.369
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–564 Fragment:UNP residues 1-564 Nucleoporin SEH1 × 1 (P53011) X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;289 K;18% PEG 3350, 0.1M Bis Tris propane, 0.2M Sodium Citrate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 3.50 Å R-free 0.369
3 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–564 Chain D; UniProt 1–564 Fragment:UNP residues 1-564 Nucleoporin SEH1 × 2 (P53011) X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;289 K;18% PEG 3350, 0.1M Bis Tris propane, 0.2M Sodium Citrate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 3.50 Å R-free 0.369

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 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NUP85_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–564; UniProt 1–564 Author chain D; PDBConstruct 1–564; UniProt 1–564

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 3ewe

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3ewe
Deposition date deposition_date2008-10-14
Structure title titleCrystal Structure of the Nup85/Seh1 Complex
Keywords keywords;Nucleoporin, Nuclear Pore Complex, mRNA transport, Nucleus, Protein transport, Translocation, Cell membrane, Membrane, Phosphoprotein, Transport, WD repeat, MEMBRANE PROTEIN, STRUCTURAL PROTEIN ;; PROTEIN TRANSPORT,STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier41.13
Radius of gyration Rg (electron density) rg_electron40.87
Forward intensity I(0) i0265152000.00
Molecular weight molecular_weight137330.0 kDa
Excluded volume excluded_volume173300 ų
Envelope volume envelope_volume240750 ų
Hydration-shell volume shell_volume50816 ų
Envelope diameter envelope_diameter152.8
Shell Rg shell_rg44.29
Envelope Rg envelope_rg40.79
Shape Rg shape_rg40.89
Total Rg total_rg40.99
Total atoms total_atoms9689
Residues n_residues1300
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 dmax146.7
Rg (real space) rg_real41.41
Rg uncertainty (real space) rg_real_error1.55
I(0) (real space) i0_real2.6520e+08
I(0) uncertainty (real space) i0_real_error5.0340e+06
Rg (reciprocal space) rg_reciprocal41.13
I(0) (reciprocal space) i0_reciprocal265100000.0000
Solution quality estimate total_estimate0.8300
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary38.6
Skewness Skewness skewness0.555
Kurtosis Kurtosis kurtosis-0.214
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha59020000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.707; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.900; Smooth: 0.765

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id3eweA01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id3eweC01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase

8. Citations (1)

9. Files and Curves (10)