4xmm

Structure of the yeast coat nucleoporin complex, space group C2

Method: X-RAY DIFFRACTION Dmax: 289.3 Å Quality: GOOD

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

Protein transport protein SEC13

Saccharomyces cerevisiae S288c

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–297 Not recorded Nucleoporin NUP145 × 1 (P49687) Nucleoporin SEH1 × 1 (P53011) Nucleoporin NUP85 × 1 (P46673) Nucleoporin NUP120 × 1 (P35729) Nucleoporin NUP84 × 1 (P52891) Antibody 57 heavy chain × 1 Antibody 57 light chain × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;PEG 20000, ethanol, MES Resolution 7.38 Å R-free 0.353

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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–297; UniProt 1–297

Nucleoporin NUP145

Saccharomyces cerevisiae S288c

UniProt P49687

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 B; UniProt 680–1317 Not recorded Protein transport protein SEC13 × 1 (Q04491) Nucleoporin SEH1 × 1 (P53011) Nucleoporin NUP85 × 1 (P46673) Nucleoporin NUP120 × 1 (P35729) Nucleoporin NUP84 × 1 (P52891) Antibody 57 heavy chain × 1 Antibody 57 light chain × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;PEG 20000, ethanol, MES Resolution 7.38 Å R-free 0.353

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.

10 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NU145_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 15–652; UniProt 680–1317

Nucleoporin SEH1

Saccharomyces cerevisiae S288c

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 C; UniProt 1–349 Not recorded Protein transport protein SEC13 × 1 (Q04491) Nucleoporin NUP145 × 1 (P49687) Nucleoporin NUP85 × 1 (P46673) Nucleoporin NUP120 × 1 (P35729) Nucleoporin NUP84 × 1 (P52891) Antibody 57 heavy chain × 1 Antibody 57 light chain × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;PEG 20000, ethanol, MES Resolution 7.38 Å R-free 0.353

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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–349; UniProt 1–349

Nucleoporin NUP85

Saccharomyces cerevisiae S288c

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 D; UniProt 44–744 Not recorded Protein transport protein SEC13 × 1 (Q04491) Nucleoporin NUP145 × 1 (P49687) Nucleoporin SEH1 × 1 (P53011) Nucleoporin NUP120 × 1 (P35729) Nucleoporin NUP84 × 1 (P52891) Antibody 57 heavy chain × 1 Antibody 57 light chain × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;PEG 20000, ethanol, MES Resolution 7.38 Å R-free 0.353

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 4
Chains and sequence ranges Author chain D; PDBConstruct 15–715; UniProt 44–744

Nucleoporin NUP120

Saccharomyces cerevisiae S288c

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 2–1037 Not recorded Protein transport protein SEC13 × 1 (Q04491) Nucleoporin NUP145 × 1 (P49687) Nucleoporin SEH1 × 1 (P53011) Nucleoporin NUP85 × 1 (P46673) Nucleoporin NUP84 × 1 (P52891) Antibody 57 heavy chain × 1 Antibody 57 light chain × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;PEG 20000, ethanol, MES Resolution 7.38 Å R-free 0.353

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 5
Chains and sequence ranges Author chain E; PDBConstruct 10–1045; UniProt 2–1037

Nucleoporin NUP84

Saccharomyces cerevisiae S288c

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain F; UniProt 1–451 Not recorded Protein transport protein SEC13 × 1 (Q04491) Nucleoporin NUP145 × 1 (P49687) Nucleoporin SEH1 × 1 (P53011) Nucleoporin NUP85 × 1 (P46673) Nucleoporin NUP120 × 1 (P35729) Antibody 57 heavy chain × 1 Antibody 57 light chain × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;PEG 20000, ethanol, MES Resolution 7.38 Å R-free 0.353

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 4–454; UniProt 1–451

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 4xmm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4xmm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4xmm
Deposition date deposition_date2015-01-14
Structure title titleStructure of the yeast coat nucleoporin complex, space group C2
Keywords keywordsStructural protein, Immune System, Transport Protein-Immune System complex; Transport Protein/Immune System
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier90.77
Radius of gyration Rg (electron density) rg_electron92.75
Forward intensity I(0) i01905540000.00
Molecular weight molecular_weight370050.0 kDa
Excluded volume excluded_volume462550 ų
Envelope volume envelope_volume850800 ų
Hydration-shell volume shell_volume86692 ų
Envelope diameter envelope_diameter283.0
Shell Rg shell_rg68.16
Envelope Rg envelope_rg88.76
Shape Rg shape_rg92.67
Total Rg total_rg92.70
Total atoms total_atoms26139
Residues n_residues3454
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 dmax289.3
Rg (real space) rg_real93.81
Rg uncertainty (real space) rg_real_error1.83
I(0) (real space) i0_real1.9060e+09
I(0) uncertainty (real space) i0_real_error4.5810e+07
Rg (reciprocal space) rg_reciprocal87.92
I(0) (reciprocal space) i0_reciprocal1888000000.0000
Solution quality estimate total_estimate0.8368
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary51.0
Skewness Skewness skewness0.231
Kurtosis Kurtosis kurtosis-0.836
Angular range angular_range— – 0.0850 −1
Current regularization parameter α current_alpha1.1630
Highest regularization parameter α highest_alpha46410000.0000
Real-space data points n_real_points18
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.838; Stabil: 0.911; Sysdev: 1.000; Positv: 1.000; Valcen: 0.891; 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)