7wot

Cryo-EM structure of the inner ring monomer of the Saccharomyces cerevisiae nuclear pore complex

Method: ELECTRON MICROSCOPY Dmax: 274.2 Å Quality: EXCELLENT

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

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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain A; UniProt 1–839 Chain M; UniProt 1–839 Chain N; UniProt 1–839 Chain Z; UniProt 1–839 Not recorded Nucleoporin NUP157 × 2 (P40064) Nucleoporin NUP170 × 2 (P38181) Nucleoporin NUP188 × 2 (P52593) Nucleoporin NUP192 × 2 (P47054) Nucleoporin NUP49/NSP49 × 4 (Q02199) Nucleoporin NUP57 × 4 (P48837) Nucleoporin NSP1 × 4 (P14907) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.73 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–839; UniProt 1–839 Author chain M; PDBConstruct 1–839; UniProt 1–839 Author chain N; PDBConstruct 1–839; UniProt 1–839 Author chain Z; PDBConstruct 1–839; UniProt 1–839

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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain C; UniProt 1–1391 Chain O; UniProt 1–1391 Not recorded Nucleoporin NIC96 × 4 (P34077) Nucleoporin NUP170 × 2 (P38181) Nucleoporin NUP188 × 2 (P52593) Nucleoporin NUP192 × 2 (P47054) Nucleoporin NUP49/NSP49 × 4 (Q02199) Nucleoporin NUP57 × 4 (P48837) Nucleoporin NSP1 × 4 (P14907) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.73 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 2
Chains and sequence ranges Author chain C; PDBConstruct 1–1391; UniProt 1–1391 Author chain O; PDBConstruct 1–1391; UniProt 1–1391

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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain D; UniProt 1–1502 Chain P; UniProt 1–1502 Not recorded Nucleoporin NIC96 × 4 (P34077) Nucleoporin NUP157 × 2 (P40064) Nucleoporin NUP188 × 2 (P52593) Nucleoporin NUP192 × 2 (P47054) Nucleoporin NUP49/NSP49 × 4 (Q02199) Nucleoporin NUP57 × 4 (P48837) Nucleoporin NSP1 × 4 (P14907) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.73 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 3
Chains and sequence ranges Author chain D; PDBConstruct 1–1502; UniProt 1–1502 Author chain P; PDBConstruct 1–1502; UniProt 1–1502

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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain E; UniProt 1–1655 Chain Q; UniProt 1–1655 Not recorded Nucleoporin NIC96 × 4 (P34077) Nucleoporin NUP157 × 2 (P40064) Nucleoporin NUP170 × 2 (P38181) Nucleoporin NUP192 × 2 (P47054) Nucleoporin NUP49/NSP49 × 4 (Q02199) Nucleoporin NUP57 × 4 (P48837) Nucleoporin NSP1 × 4 (P14907) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.73 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 4
Chains and sequence ranges Author chain E; PDBConstruct 1–1655; UniProt 1–1655 Author chain Q; PDBConstruct 1–1655; UniProt 1–1655

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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain F; UniProt 1–1683 Chain R; UniProt 1–1683 Not recorded Nucleoporin NIC96 × 4 (P34077) Nucleoporin NUP157 × 2 (P40064) Nucleoporin NUP170 × 2 (P38181) Nucleoporin NUP188 × 2 (P52593) Nucleoporin NUP49/NSP49 × 4 (Q02199) Nucleoporin NUP57 × 4 (P48837) Nucleoporin NSP1 × 4 (P14907) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.73 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 5
Chains and sequence ranges Author chain F; PDBConstruct 1–1683; UniProt 1–1683 Author chain R; PDBConstruct 1–1683; UniProt 1–1683

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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain G; UniProt 1–472 Chain J; UniProt 1–472 Chain S; UniProt 1–472 Chain V; UniProt 1–472 Not recorded Nucleoporin NIC96 × 4 (P34077) Nucleoporin NUP157 × 2 (P40064) Nucleoporin NUP170 × 2 (P38181) Nucleoporin NUP188 × 2 (P52593) Nucleoporin NUP192 × 2 (P47054) Nucleoporin NUP57 × 4 (P48837) Nucleoporin NSP1 × 4 (P14907) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.73 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 G; PDBConstruct 1–472; UniProt 1–472 Author chain J; PDBConstruct 1–472; UniProt 1–472 Author chain S; PDBConstruct 1–472; UniProt 1–472 Author chain V; PDBConstruct 1–472; UniProt 1–472

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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain H; UniProt 1–541 Chain K; UniProt 1–541 Chain T; UniProt 1–541 Chain W; UniProt 1–541 Not recorded Nucleoporin NIC96 × 4 (P34077) Nucleoporin NUP157 × 2 (P40064) Nucleoporin NUP170 × 2 (P38181) Nucleoporin NUP188 × 2 (P52593) Nucleoporin NUP192 × 2 (P47054) Nucleoporin NUP49/NSP49 × 4 (Q02199) Nucleoporin NSP1 × 4 (P14907) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.73 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 7
Chains and sequence ranges Author chain H; PDBConstruct 1–541; UniProt 1–541 Author chain K; PDBConstruct 1–541; UniProt 1–541 Author chain T; PDBConstruct 1–541; UniProt 1–541 Author chain W; PDBConstruct 1–541; UniProt 1–541

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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain I; UniProt 1–823 Chain L; UniProt 1–823 Chain U; UniProt 1–823 Chain X; UniProt 1–823 Not recorded Nucleoporin NIC96 × 4 (P34077) Nucleoporin NUP157 × 2 (P40064) Nucleoporin NUP170 × 2 (P38181) Nucleoporin NUP188 × 2 (P52593) Nucleoporin NUP192 × 2 (P47054) Nucleoporin NUP49/NSP49 × 4 (Q02199) Nucleoporin NUP57 × 4 (P48837) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.73 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 8
Chains and sequence ranges Author chain I; PDBConstruct 1–823; UniProt 1–823 Author chain L; PDBConstruct 1–823; UniProt 1–823 Author chain U; PDBConstruct 1–823; UniProt 1–823 Author chain X; PDBConstruct 1–823; UniProt 1–823

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 7wot

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7wot
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7wot
Deposition date deposition_date2022-01-22
Structure title titleCryo-EM structure of the inner ring monomer of the Saccharomyces cerevisiae nuclear pore complex
Keywords keywordsnuclear pore complex, inner ring, monomer, Saccharomyces cerevisiae, 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_electron105.30
Forward intensity I(0) i047132400000.00
Molecular weight molecular_weight1896100.0 kDa
Excluded volume excluded_volume2388000 ų
Envelope volume envelope_volume4895400 ų
Hydration-shell volume shell_volume387940 ų
Envelope diameter envelope_diameter407.1
Shell Rg shell_rg105.70
Envelope Rg envelope_rg100.00
Shape Rg shape_rg105.30
Total Rg total_rg105.40
Total atoms total_atoms133827
Residues n_residues17285
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 dmax274.2
Rg (real space) rg_real100.70
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real4.4830e+10
I(0) uncertainty (real space) i0_real_error8.5150e+08
Rg (reciprocal space) rg_reciprocal106.90
I(0) (reciprocal space) i0_reciprocal47390000000.0000
Solution quality estimate total_estimate0.9075
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary127.9
Skewness Skewness skewness0.075
Kurtosis Kurtosis kurtosis-0.505
Angular range angular_range— – 0.0750 −1
Current regularization parameter α current_alpha0.8603
Highest regularization parameter α highest_alpha3535000000.0000
Real-space data points n_real_points16
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.002; Oscil: 0.996; Stabil: 0.964; Sysdev: 1.000; Positv: 1.000; Valcen: 0.919; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)