8tj5

Inner spoke ring of the yeast NPC

Method: ELECTRON MICROSCOPY Dmax: 274.9 Å Quality: EXCELLENT

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

Nucleoporin NUP170

OrganismNot specified

UniProt P38181

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 × 46 PDB declaration: 46-meric(46) Consistent with protein copy count Chain 0; UniProt 1–1502 Chain Y; UniProt 1–1502 Not recorded Spoke connector × 18 Nucleoporin NUP157 × 2 (P40064) Nucleoporin NSP1 × 4 (P14907) Nucleoporin NUP57 × 4 (P48837) Nucleoporin NUP49/NSP49 × 4 (Q02199) Nucleoporin NUP192 × 2 (P47054) Nucleoporin NUP188 × 2 (P52593) Nucleoporin NIC96 × 4 (P34077) Nucleoporin NUP53 × 2 (Q03790) Nucleoporin 59 × 2 (Q05166) 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 6.60 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.

6 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NU170_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain 0; PDBConstruct 1–1502; UniProt 1–1502 Author chain Y; PDBConstruct 1–1502; UniProt 1–1502

Nucleoporin NUP157

OrganismNot specified

UniProt P40064

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 × 46 PDB declaration: 46-meric(46) Consistent with protein copy count Chain 1; UniProt 1–1391 Chain Z; UniProt 1–1391 Not recorded Spoke connector × 18 Nucleoporin NUP170 × 2 (P38181) Nucleoporin NSP1 × 4 (P14907) Nucleoporin NUP57 × 4 (P48837) Nucleoporin NUP49/NSP49 × 4 (Q02199) Nucleoporin NUP192 × 2 (P47054) Nucleoporin NUP188 × 2 (P52593) Nucleoporin NIC96 × 4 (P34077) Nucleoporin NUP53 × 2 (Q03790) Nucleoporin 59 × 2 (Q05166) 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 6.60 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.

5 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NU157_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain 1; PDBConstruct 1–1391; UniProt 1–1391 Author chain Z; PDBConstruct 1–1391; UniProt 1–1391

Nucleoporin NSP1

OrganismNot specified

UniProt P14907

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 × 46 PDB declaration: 46-meric(46) Consistent with protein copy count Chain A; UniProt 1–823 Chain D; UniProt 1–823 Chain G; UniProt 1–823 Chain J; UniProt 1–823 Not recorded Spoke connector × 18 Nucleoporin NUP170 × 2 (P38181) Nucleoporin NUP157 × 2 (P40064) Nucleoporin NUP57 × 4 (P48837) Nucleoporin NUP49/NSP49 × 4 (Q02199) Nucleoporin NUP192 × 2 (P47054) Nucleoporin NUP188 × 2 (P52593) Nucleoporin NIC96 × 4 (P34077) Nucleoporin NUP53 × 2 (Q03790) Nucleoporin 59 × 2 (Q05166) 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 6.60 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.

5 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NSP1_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain A; PDBConstruct 1–823; UniProt 1–823 Author chain D; PDBConstruct 1–823; UniProt 1–823 Author chain G; PDBConstruct 1–823; UniProt 1–823 Author chain J; PDBConstruct 1–823; UniProt 1–823

Nucleoporin NUP57

OrganismNot specified

UniProt P48837

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 × 46 PDB declaration: 46-meric(46) Consistent with protein copy count Chain B; UniProt 1–541 Chain E; UniProt 1–541 Chain H; UniProt 1–541 Chain K; UniProt 1–541 Not recorded Spoke connector × 18 Nucleoporin NUP170 × 2 (P38181) Nucleoporin NUP157 × 2 (P40064) Nucleoporin NSP1 × 4 (P14907) Nucleoporin NUP49/NSP49 × 4 (Q02199) Nucleoporin NUP192 × 2 (P47054) Nucleoporin NUP188 × 2 (P52593) Nucleoporin NIC96 × 4 (P34077) Nucleoporin NUP53 × 2 (Q03790) Nucleoporin 59 × 2 (Q05166) 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 6.60 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.

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

View Construct and Data Evidence
UniProt name NUP57_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain B; PDBConstruct 1–541; UniProt 1–541 Author chain E; PDBConstruct 1–541; UniProt 1–541 Author chain H; PDBConstruct 1–541; UniProt 1–541 Author chain K; PDBConstruct 1–541; UniProt 1–541

Nucleoporin NUP49/NSP49

OrganismNot specified

UniProt Q02199

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 × 46 PDB declaration: 46-meric(46) Consistent with protein copy count Chain C; UniProt 1–472 Chain F; UniProt 1–472 Chain I; UniProt 1–472 Chain L; UniProt 1–472 Not recorded Spoke connector × 18 Nucleoporin NUP170 × 2 (P38181) Nucleoporin NUP157 × 2 (P40064) Nucleoporin NSP1 × 4 (P14907) Nucleoporin NUP57 × 4 (P48837) Nucleoporin NUP192 × 2 (P47054) Nucleoporin NUP188 × 2 (P52593) Nucleoporin NIC96 × 4 (P34077) Nucleoporin NUP53 × 2 (Q03790) Nucleoporin 59 × 2 (Q05166) 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 6.60 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.

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

View Construct and Data Evidence
UniProt name NUP49_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain C; PDBConstruct 1–472; UniProt 1–472 Author chain F; PDBConstruct 1–472; UniProt 1–472 Author chain I; PDBConstruct 1–472; UniProt 1–472 Author chain L; PDBConstruct 1–472; UniProt 1–472

Nucleoporin NUP192

OrganismNot specified

UniProt P47054

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 × 46 PDB declaration: 46-meric(46) Consistent with protein copy count Chain M; UniProt 1–1683 Chain O; UniProt 1–1683 Not recorded Spoke connector × 18 Nucleoporin NUP170 × 2 (P38181) Nucleoporin NUP157 × 2 (P40064) Nucleoporin NSP1 × 4 (P14907) Nucleoporin NUP57 × 4 (P48837) Nucleoporin NUP49/NSP49 × 4 (Q02199) Nucleoporin NUP188 × 2 (P52593) Nucleoporin NIC96 × 4 (P34077) Nucleoporin NUP53 × 2 (Q03790) Nucleoporin 59 × 2 (Q05166) 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 6.60 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.

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

View Construct and Data Evidence
UniProt name NU192_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain M; PDBConstruct 1–1683; UniProt 1–1683 Author chain O; PDBConstruct 1–1683; UniProt 1–1683

Nucleoporin NUP188

OrganismNot specified

UniProt P52593

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 × 46 PDB declaration: 46-meric(46) Consistent with protein copy count Chain N; UniProt 1–1655 Chain P; UniProt 1–1655 Not recorded Spoke connector × 18 Nucleoporin NUP170 × 2 (P38181) Nucleoporin NUP157 × 2 (P40064) Nucleoporin NSP1 × 4 (P14907) Nucleoporin NUP57 × 4 (P48837) Nucleoporin NUP49/NSP49 × 4 (Q02199) Nucleoporin NUP192 × 2 (P47054) Nucleoporin NIC96 × 4 (P34077) Nucleoporin NUP53 × 2 (Q03790) Nucleoporin 59 × 2 (Q05166) 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 6.60 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.

6 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NU188_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain N; PDBConstruct 1–1655; UniProt 1–1655 Author chain P; PDBConstruct 1–1655; UniProt 1–1655

Nucleoporin NIC96

OrganismNot specified

UniProt P34077

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 × 46 PDB declaration: 46-meric(46) Consistent with protein copy count Chain Q; UniProt 1–839 Chain R; UniProt 1–839 Chain S; UniProt 1–839 Chain T; UniProt 1–839 Not recorded Spoke connector × 18 Nucleoporin NUP170 × 2 (P38181) Nucleoporin NUP157 × 2 (P40064) Nucleoporin NSP1 × 4 (P14907) Nucleoporin NUP57 × 4 (P48837) Nucleoporin NUP49/NSP49 × 4 (Q02199) Nucleoporin NUP192 × 2 (P47054) Nucleoporin NUP188 × 2 (P52593) Nucleoporin NUP53 × 2 (Q03790) Nucleoporin 59 × 2 (Q05166) 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 6.60 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.

7 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NIC96_YEAST
Isoform
PDB entities 9
Chains and sequence ranges Author chain Q; PDBConstruct 1–839; UniProt 1–839 Author chain R; PDBConstruct 1–839; UniProt 1–839 Author chain S; PDBConstruct 1–839; UniProt 1–839 Author chain T; PDBConstruct 1–839; UniProt 1–839

Nucleoporin NUP53

OrganismNot specified

UniProt Q03790

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 × 46 PDB declaration: 46-meric(46) Consistent with protein copy count Chain U; UniProt 1–475 Chain W; UniProt 1–475 Not recorded Spoke connector × 18 Nucleoporin NUP170 × 2 (P38181) Nucleoporin NUP157 × 2 (P40064) Nucleoporin NSP1 × 4 (P14907) Nucleoporin NUP57 × 4 (P48837) Nucleoporin NUP49/NSP49 × 4 (Q02199) Nucleoporin NUP192 × 2 (P47054) Nucleoporin NUP188 × 2 (P52593) Nucleoporin NIC96 × 4 (P34077) Nucleoporin 59 × 2 (Q05166) 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 6.60 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.

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

View Construct and Data Evidence
UniProt name NUP53_YEAST
Isoform
PDB entities 10
Chains and sequence ranges Author chain U; PDBConstruct 1–475; UniProt 1–475 Author chain W; PDBConstruct 1–475; UniProt 1–475

Nucleoporin 59

OrganismNot specified

UniProt Q05166

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 × 46 PDB declaration: 46-meric(46) Consistent with protein copy count Chain V; UniProt 1–528 Chain X; UniProt 1–528 Not recorded Spoke connector × 18 Nucleoporin NUP170 × 2 (P38181) Nucleoporin NUP157 × 2 (P40064) Nucleoporin NSP1 × 4 (P14907) Nucleoporin NUP57 × 4 (P48837) Nucleoporin NUP49/NSP49 × 4 (Q02199) Nucleoporin NUP192 × 2 (P47054) Nucleoporin NUP188 × 2 (P52593) Nucleoporin NIC96 × 4 (P34077) Nucleoporin NUP53 × 2 (Q03790) 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 6.60 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.

2 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NUP59_YEAST
Isoform
PDB entities 11
Chains and sequence ranges Author chain V; PDBConstruct 1–528; UniProt 1–528 Author chain X; PDBConstruct 1–528; UniProt 1–528

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 8tj5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8tj5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8tj5
Deposition date deposition_date2023-07-20
最后修订 last_revision2023-10-11
Structure title titleInner spoke ring of 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_electron105.70
Forward intensity I(0) i049433600000.00
Molecular weight molecular_weight1959400.0 kDa
Excluded volume excluded_volume2474800 ų
Envelope volume envelope_volume4900200 ų
Hydration-shell volume shell_volume386000 ų
Envelope diameter envelope_diameter397.3
Shell Rg shell_rg105.40
Envelope Rg envelope_rg100.70
Shape Rg shape_rg105.70
Total Rg total_rg105.70
Total atoms total_atoms138272
Residues n_residues17560
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 dmax274.9
Rg (real space) rg_real101.40
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real4.7090e+10
I(0) uncertainty (real space) i0_real_error9.3560e+08
Rg (reciprocal space) rg_reciprocal107.30
I(0) (reciprocal space) i0_reciprocal49690000000.0000
Solution quality estimate total_estimate0.9084
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary128.3
Skewness Skewness skewness0.091
Kurtosis Kurtosis kurtosis-0.514
Angular range angular_range— – 0.0750 −1
Current regularization parameter α current_alpha0.7911
Highest regularization parameter α highest_alpha4006000000.0000
Real-space data points n_real_points16
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.997; Stabil: 0.965; Sysdev: 1.000; Positv: 1.000; Valcen: 0.925; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)