3hxr

Nucleoporin Nup120 from S.cerevisiae (aa 1-757)

Method: X-RAY DIFFRACTION Dmax: 98.1 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 1–757 Fragment:UNP residues 1-757 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;15% PEG3350, 0.2M KSCN, 0.1M Tris-HCl pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 3.00 Å R-free 0.299

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 5–761; UniProt 1–757

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 3hxr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3hxr
Deposition date deposition_date2009-06-21
Structure title titleNucleoporin Nup120 from S.cerevisiae (aa 1-757)
Keywords keywords;structural protein, Coiled coil, Membrane, mRNA transport, Nuclear pore complex, Nucleus, Phosphoprotein, Protein transport, Translocation, Transport ;; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.31
Radius of gyration Rg (electron density) rg_electron28.67
Forward intensity I(0) i086658800.00
Molecular weight molecular_weight75572.0 kDa
Excluded volume excluded_volume95212 ų
Envelope volume envelope_volume119310 ų
Hydration-shell volume shell_volume35078 ų
Envelope diameter envelope_diameter105.9
Shell Rg shell_rg35.65
Envelope Rg envelope_rg28.87
Shape Rg shape_rg28.68
Total Rg total_rg29.33
Total atoms total_atoms5313
Residues n_residues651
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 dmax98.1
Rg (real space) rg_real29.34
Rg uncertainty (real space) rg_real_error0.96
I(0) (real space) i0_real8.6660e+07
I(0) uncertainty (real space) i0_real_error1.4390e+06
Rg (reciprocal space) rg_reciprocal29.33
I(0) (reciprocal space) i0_reciprocal86660000.0000
Solution quality estimate total_estimate0.8049
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.7
Skewness Skewness skewness0.422
Kurtosis Kurtosis kurtosis-0.232
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha27580000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.823; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)