1f59

IMPORTIN-BETA-FXFG NUCLEOPORIN COMPLEX

Method: X-RAY DIFFRACTION Dmax: 129.7 Å Quality: REASONABLE

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

IMPORTIN BETA-1

Homo sapiens

UniProt Q14974

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–442 Not recorded FXFG NUCLEOPORIN REPEATS × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;ammonium sulphate, ammonium acetate, dtt, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 20K Resolution 2.80 Å R-free 0.262
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–442 Not recorded FXFG NUCLEOPORIN REPEATS × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;ammonium sulphate, ammonium acetate, dtt, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 20K Resolution 2.80 Å R-free 0.262

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.

22 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IMB1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–442; UniProt 1–442 Author chain B; PDBConstruct 1–442; UniProt 1–442

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 1f59

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1f59
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1f59
Deposition date deposition_date2000-06-13
Structure title titleIMPORTIN-BETA-FXFG NUCLEOPORIN COMPLEX
Keywords keywordsProtein-protein complex, TRANSPORT PROTEIN RECEPTOR; TRANSPORT PROTEIN RECEPTOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier45.77
Radius of gyration Rg (electron density) rg_electron45.80
Forward intensity I(0) i0156048000.00
Molecular weight molecular_weight102070.0 kDa
Excluded volume excluded_volume127660 ų
Envelope volume envelope_volume201650 ų
Hydration-shell volume shell_volume38638 ų
Envelope diameter envelope_diameter138.8
Shell Rg shell_rg47.89
Envelope Rg envelope_rg43.33
Shape Rg shape_rg45.85
Total Rg total_rg45.72
Total atoms total_atoms7158
Residues n_residues922
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 dmax129.7
Rg (real space) rg_real46.07
Rg uncertainty (real space) rg_real_error1.08
I(0) (real space) i0_real1.5600e+08
I(0) uncertainty (real space) i0_real_error2.6330e+06
Rg (reciprocal space) rg_reciprocal45.77
I(0) (reciprocal space) i0_reciprocal156000000.0000
Solution quality estimate total_estimate0.5712
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.5
Skewness Skewness skewness0.243
Kurtosis Kurtosis kurtosis-1.018
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5187000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.867; Stabil: 0.999; Sysdev: 0.115; Positv: 1.000; Valcen: 0.477; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1f59a_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.1 — Armadillo repeat
Domain ID domain_idd1f59b_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.1 — Armadillo repeat
Domain ID domain_idd1f59c_
Class classj — Peptides
Fold Fold foldj.70 — FxFG nucleoporin repeats
Superfamily Superfamily superfamilyj.70.1 — FxFG nucleoporin repeats
Family Family familyj.70.1.1 — FxFG nucleoporin repeats
Domain ID domain_idd1f59d_
Class classj — Peptides
Fold Fold foldj.70 — FxFG nucleoporin repeats
Superfamily Superfamily superfamilyj.70.1 — FxFG nucleoporin repeats
Family Family familyj.70.1.1 — FxFG nucleoporin repeats

CATH v4.4 (2 domains)

Domain ID domain_id1f59A00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant
Domain ID domain_id1f59B00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant

8. Citations (1)

9. Files and Curves (10)