3f7f

Structure of Nup120

Method: X-RAY DIFFRACTION Dmax: 197.2 Å Quality: GOOD

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

Nucleoporin NUP120

Saccharomyces cerevisiae

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–729 Fragment:UNP residues 1-729 Mutation:S207C HG MERCURY (II) ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;Succinic acid, PEG 3350, Sodium bromide, Ethylene glycol, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.60 Å R-free 0.254
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–729 Fragment:UNP residues 1-729 Mutation:S207C HG MERCURY (II) ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;Succinic acid, PEG 3350, Sodium bromide, Ethylene glycol, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.60 Å R-free 0.254
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 1–729 Fragment:UNP residues 1-729 Mutation:S207C HG MERCURY (II) ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;Succinic acid, PEG 3350, Sodium bromide, Ethylene glycol, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.60 Å R-free 0.254
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 1–729 Fragment:UNP residues 1-729 Mutation:S207C HG MERCURY (II) ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;Succinic acid, PEG 3350, Sodium bromide, Ethylene glycol, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.60 Å R-free 0.254
5 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–729 Chain B; UniProt 1–729 Fragment:UNP residues 1-729 Mutation:S207C HG MERCURY (II) ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;Succinic acid, PEG 3350, Sodium bromide, Ethylene glycol, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.60 Å R-free 0.254
6 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–729 Chain D; UniProt 1–729 Fragment:UNP residues 1-729 Mutation:S207C HG MERCURY (II) ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;Succinic acid, PEG 3350, Sodium bromide, Ethylene glycol, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.60 Å R-free 0.254

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 15 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 1–729; UniProt 1–729 Author chain B; PDBConstruct 1–729; UniProt 1–729 Author chain C; PDBConstruct 1–729; UniProt 1–729 Author chain D; PDBConstruct 1–729; UniProt 1–729

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 3f7f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3f7f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3f7f
Deposition date deposition_date2008-11-08
Structure title titleStructure of Nup120
Keywords keywords;Nucleoporin, Nuclear Pore Complex, Macromolecular Assembly, Membrane Coat, Nucleocytoplasmic Transport, beta-propeller, alpha-helical solenoid domain, Coiled coil, mRNA transport, Nucleus, Protein transport, Translocation, STRUCTURAL PROTEIN ;; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier56.72
Radius of gyration Rg (electron density) rg_electron56.86
Forward intensity I(0) i01414460000.00
Molecular weight molecular_weight325870.0 kDa
Excluded volume excluded_volume410620 ų
Envelope volume envelope_volume591920 ų
Hydration-shell volume shell_volume87731 ų
Envelope diameter envelope_diameter198.0
Shell Rg shell_rg57.97
Envelope Rg envelope_rg55.76
Shape Rg shape_rg56.88
Total Rg total_rg56.84
Total atoms total_atoms22876
Residues n_residues2804
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 dmax197.2
Rg (real space) rg_real56.82
Rg uncertainty (real space) rg_real_error2.44
I(0) (real space) i0_real1.4140e+09
I(0) uncertainty (real space) i0_real_error2.8340e+07
Rg (reciprocal space) rg_reciprocal56.61
I(0) (reciprocal space) i0_reciprocal1414000000.0000
Solution quality estimate total_estimate0.8707
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary70.4
Skewness Skewness skewness0.313
Kurtosis Kurtosis kurtosis-0.452
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha123200000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.854; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.972; Smooth: 0.780

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)