3f3g

Crystal structure of the nucleoporin pair Nup85-Seh1, space group P212121

Method: X-RAY DIFFRACTION Dmax: 223.3 Å Quality: REASONABLE

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–349 Chain B; UniProt 1–349 Chain E; UniProt 1–349 Chain F; UniProt 1–349 Not recorded Nucleoporin NUP85 × 4 (P46673) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;Sodium citrate, Sodium chloride, Tris-HCl buffer, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.75 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.

9 other PDB entries and 17 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 3–351; UniProt 1–349 Author chain B; PDBConstruct 3–351; UniProt 1–349 Author chain E; PDBConstruct 3–351; UniProt 1–349 Author chain F; PDBConstruct 3–351; 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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain C; UniProt 1–570 Chain D; UniProt 1–570 Chain G; UniProt 1–570 Chain H; UniProt 1–570 Fragment:UNP residues 1-570 Nucleoporin SEH1 × 4 (P53011) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;Sodium citrate, Sodium chloride, Tris-HCl buffer, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.75 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.

9 other PDB entries and 17 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 C; PDBConstruct 1–570; UniProt 1–570 Author chain D; PDBConstruct 1–570; UniProt 1–570 Author chain G; PDBConstruct 1–570; UniProt 1–570 Author chain H; PDBConstruct 1–570; UniProt 1–570

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 3f3g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3f3g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3f3g
Deposition date deposition_date2008-10-30
Structure title titleCrystal structure of the nucleoporin pair Nup85-Seh1, space group P212121
Keywords keywords;Structural Protein, Protein Complex, Nucleoporin, Nucleoporin Complex, Nuclear Pore Complex, Macromolecular Assembly, Membrane Coat, Nucleocytoplasmic Transport, beta-propeller, solenoid domain, mRNA transport, Nucleus, Protein transport, Translocation, WD repeat ;; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier76.24
Radius of gyration Rg (electron density) rg_electron77.07
Forward intensity I(0) i01716390000.00
Molecular weight molecular_weight356620.0 kDa
Excluded volume excluded_volume448080 ų
Envelope volume envelope_volume700120 ų
Hydration-shell volume shell_volume79712 ų
Envelope diameter envelope_diameter302.1
Shell Rg shell_rg69.29
Envelope Rg envelope_rg75.14
Shape Rg shape_rg77.08
Total Rg total_rg76.94
Total atoms total_atoms25114
Residues n_residues3147
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 dmax223.3
Rg (real space) rg_real75.66
Rg uncertainty (real space) rg_real_error1.65
I(0) (real space) i0_real1.7040e+09
I(0) uncertainty (real space) i0_real_error3.8300e+07
Rg (reciprocal space) rg_reciprocal72.77
I(0) (reciprocal space) i0_reciprocal1701000000.0000
Solution quality estimate total_estimate0.7318
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary44.6
Skewness Skewness skewness0.421
Kurtosis Kurtosis kurtosis-0.876
Angular range angular_range— – 0.1000 −1
Current regularization parameter α current_alpha0.0316
Highest regularization parameter α highest_alpha40220000.0000
Real-space data points n_real_points21
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.616; Stabil: 0.989; Sysdev: 1.000; Positv: 1.000; Valcen: 0.661; Smooth: 0.004

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id3f3gA01
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_id3f3gB01
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_id3f3gE01
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_id3f3gF01
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)