8tie

Double nuclear outer ring of Nup84-complexes from the yeast NPC

Method: ELECTRON MICROSCOPY Dmax: 405.4 Å Quality: GOOD

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

Nucleoporin NUP120

OrganismNot specified

UniProt P35729

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain a; UniProt 1–1037 Chain l; UniProt 1–1037 Not recorded Nucleoporin NUP85 × 2 (P46673) NUP145 isoform 1 × 2 (A0A8H4C085) Protein transport protein SEC13 × 2 (Q04491) Nucleoporin Seh1 × 2 Nucleoporin NUP84 × 2 (P52891) NUP133 isoform 1 × 2 (A0A6V8RYD2) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20mM HEPES,50mM Potassium acetate,20mM NaCl,2mM MgCl2,1mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.10 Å

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.

8 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NU120_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain a; PDBConstruct 1–1037; UniProt 1–1037 Author chain l; PDBConstruct 1–1037; UniProt 1–1037

Nucleoporin NUP85

OrganismNot specified

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain b; UniProt 1–744 Chain m; UniProt 1–744 Not recorded Nucleoporin NUP120 × 2 (P35729) NUP145 isoform 1 × 2 (A0A8H4C085) Protein transport protein SEC13 × 2 (Q04491) Nucleoporin Seh1 × 2 Nucleoporin NUP84 × 2 (P52891) NUP133 isoform 1 × 2 (A0A6V8RYD2) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20mM HEPES,50mM Potassium acetate,20mM NaCl,2mM MgCl2,1mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.10 Å

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 b; PDBConstruct 1–744; UniProt 1–744 Author chain m; PDBConstruct 1–744; UniProt 1–744

NUP145 isoform 1

OrganismNot specified

UniProt A0A8H4C085

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain c; UniProt 1–1317 Chain n; UniProt 1–1317 Not recorded Nucleoporin NUP120 × 2 (P35729) Nucleoporin NUP85 × 2 (P46673) Protein transport protein SEC13 × 2 (Q04491) Nucleoporin Seh1 × 2 Nucleoporin NUP84 × 2 (P52891) NUP133 isoform 1 × 2 (A0A6V8RYD2) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20mM HEPES,50mM Potassium acetate,20mM NaCl,2mM MgCl2,1mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.10 Å

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 A0A8H4C085_YEASX
Isoform
PDB entities 3
Chains and sequence ranges Author chain c; PDBConstruct 1–1317; UniProt 1–1317 Author chain n; PDBConstruct 1–1317; UniProt 1–1317

Protein transport protein SEC13

OrganismNot specified

UniProt Q04491

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain d; UniProt 1–297 Chain o; UniProt 1–297 Not recorded Nucleoporin NUP120 × 2 (P35729) Nucleoporin NUP85 × 2 (P46673) NUP145 isoform 1 × 2 (A0A8H4C085) Nucleoporin Seh1 × 2 Nucleoporin NUP84 × 2 (P52891) NUP133 isoform 1 × 2 (A0A6V8RYD2) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20mM HEPES,50mM Potassium acetate,20mM NaCl,2mM MgCl2,1mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.10 Å

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.

19 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SEC13_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain d; PDBConstruct 1–297; UniProt 1–297 Author chain o; PDBConstruct 1–297; UniProt 1–297

Nucleoporin NUP84

OrganismNot specified

UniProt P52891

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain f; UniProt 1–726 Chain q; UniProt 1–726 Not recorded Nucleoporin NUP120 × 2 (P35729) Nucleoporin NUP85 × 2 (P46673) NUP145 isoform 1 × 2 (A0A8H4C085) Protein transport protein SEC13 × 2 (Q04491) Nucleoporin Seh1 × 2 NUP133 isoform 1 × 2 (A0A6V8RYD2) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20mM HEPES,50mM Potassium acetate,20mM NaCl,2mM MgCl2,1mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.10 Å

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.

8 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NUP84_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain f; PDBConstruct 1–726; UniProt 1–726 Author chain q; PDBConstruct 1–726; UniProt 1–726

NUP133 isoform 1

OrganismNot specified

UniProt A0A6V8RYD2

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain g; UniProt 1–1157 Chain r; UniProt 1–1157 Not recorded Nucleoporin NUP120 × 2 (P35729) Nucleoporin NUP85 × 2 (P46673) NUP145 isoform 1 × 2 (A0A8H4C085) Protein transport protein SEC13 × 2 (Q04491) Nucleoporin Seh1 × 2 Nucleoporin NUP84 × 2 (P52891) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20mM HEPES,50mM Potassium acetate,20mM NaCl,2mM MgCl2,1mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.10 Å

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 A0A6V8RYD2_YEASX
Isoform
PDB entities 7
Chains and sequence ranges Author chain g; PDBConstruct 1–1157; UniProt 1–1157 Author chain r; PDBConstruct 1–1157; UniProt 1–1157

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 8tie

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8tie
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8tie
Deposition date deposition_date2023-07-19
最后修订 last_revision2023-10-11
Structure title titleDouble nuclear outer ring of Nup84-complexes from the yeast NPC
Keywords keywordsnuclear pore complex, nucleocytoplasmic transport, nucleoporin, membrane protein, translocase, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron149.00
Forward intensity I(0) i015291200000.00
Molecular weight molecular_weight1086200.0 kDa
Excluded volume excluded_volume1369900 ų
Envelope volume envelope_volume3219300 ų
Hydration-shell volume shell_volume208130 ų
Envelope diameter envelope_diameter546.6
Shell Rg shell_rg93.65
Envelope Rg envelope_rg145.80
Shape Rg shape_rg149.00
Total Rg total_rg148.70
Total atoms total_atoms76621
Residues n_residues9479
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 dmax405.4
Rg (real space) rg_real135.90
Rg uncertainty (real space) rg_real_error2.66
I(0) (real space) i0_real1.4650e+10
I(0) uncertainty (real space) i0_real_error3.5350e+08
Rg (reciprocal space) rg_reciprocal117.70
I(0) (reciprocal space) i0_reciprocal13850000000.0000
Solution quality estimate total_estimate0.8978
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary162.2
Skewness Skewness skewness0.366
Kurtosis Kurtosis kurtosis-0.629
Angular range angular_range— – 0.0500 −1
Current regularization parameter α current_alpha0.6209
Highest regularization parameter α highest_alpha518900000.0000
Real-space data points n_real_points11
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.078; Oscil: 0.944; Stabil: 0.975; Sysdev: 1.000; Positv: 1.000; Valcen: 0.909; Smooth: 0.004

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)