1pjn

Mouse Importin alpha-bipartite NLS N1N2 from Xenopus laevis phosphoprotein Complex

Method: X-RAY DIFFRACTION Dmax: 98.6 Å Quality: GOOD

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

Histone-binding protein N1/N2

OrganismNot specified

UniProt P52293

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 531–552 Fragment:NLS (nuclear localization signal) bipartite peptide Mutation:Q555G Importin alpha-2 subunit × 1 (P06180) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;Sodium Citrate, DTT, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.50 Å R-free 0.233

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.

150 other PDB entries and 151 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IMA2_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–21; UniProt 531–552

Importin alpha-2 subunit

Mus musculus

UniProt P06180

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 B; UniProt 70–529 Fragment:NLS binding domain (70-529) Histone-binding protein N1/N2 × 1 (P52293) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;Sodium Citrate, DTT, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.50 Å R-free 0.233

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name HIBN_XENLA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–460; UniProt 70–529

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 1pjn

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1pjn
Deposition date deposition_date2003-06-03
Structure title titleMouse Importin alpha-bipartite NLS N1N2 from Xenopus laevis phosphoprotein Complex
Keywords keywords;IMPORTIN ALPHA/KARYOPHERIN ALPHA, NUCLEAR LOCALIZATION SEQUENCE (NLS) RECOGNITION, BIPARTITE NLS, Xenopus laevis N1N2 phosphoprotein, PROTEIN TRANSPORT ;; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.98
Radius of gyration Rg (electron density) rg_electron27.76
Forward intensity I(0) i036302100.00
Molecular weight molecular_weight48332.0 kDa
Excluded volume excluded_volume61185 ų
Envelope volume envelope_volume73280 ų
Hydration-shell volume shell_volume23895 ų
Envelope diameter envelope_diameter101.6
Shell Rg shell_rg32.56
Envelope Rg envelope_rg27.88
Shape Rg shape_rg27.77
Total Rg total_rg28.25
Total atoms total_atoms3402
Residues n_residues447
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 dmax98.6
Rg (real space) rg_real28.34
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real3.6300e+07
I(0) uncertainty (real space) i0_real_error4.8300e+05
Rg (reciprocal space) rg_reciprocal28.23
I(0) (reciprocal space) i0_reciprocal36300000.0000
Solution quality estimate total_estimate0.7947
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.2
Skewness Skewness skewness0.563
Kurtosis Kurtosis kurtosis-0.341
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16390000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.622; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.556; Smooth: 0.906

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1pjnb_
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

CATH v4.4 (1 domains)

Domain ID domain_id1pjnB00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant

8. Citations (4)

9. Files and Curves (10)