1ejy

MOUSE IMPORTIN ALPHA-NUCLEOPLASMIN NLS PEPTIDE COMPLEX

Method: X-RAY DIFFRACTION Dmax: 99.3 Å Quality: GOOD

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

NUCLEOPLASMIN NLS PEPTIDE

OrganismNot specified

UniProt P05221

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 N; UniProt 155–170 Fragment:NLS (NUCLEAR LOCALIZATION SIGNAL) BIPARTITE PEPTIDE, RESIDUES 155-170 IMPORTIN ALPHA × 1 (P52293) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;sodium citrate, Hepes, DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.90 Å R-free 0.268

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NUPL_XENLA
Isoform
PDB entities 1
Chains and sequence ranges Author chain N; PDBConstruct 1–16; UniProt 155–170

IMPORTIN ALPHA

Mus musculus

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 I; UniProt 70–529 Fragment:NLS BINDING DOMAIN, RESIDUES 70-529 NUCLEOPLASMIN NLS PEPTIDE × 1 (P05221) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;sodium citrate, Hepes, DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.90 Å R-free 0.268

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 2
Chains and sequence ranges Author chain I; 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 1ejy

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ejy
Deposition date deposition_date2000-03-05
Structure title titleMOUSE IMPORTIN ALPHA-NUCLEOPLASMIN NLS PEPTIDE COMPLEX
Keywords keywords;importin aplpha/karyopherin alpha; nuclear localization sequence (NLS) recognition; nucleoplasmin, PROTEIN BINDING, Hydrolase-Peptide complex ;; Hydrolase/Peptide
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.09
Radius of gyration Rg (electron density) rg_electron27.88
Forward intensity I(0) i035351800.00
Molecular weight molecular_weight47822.0 kDa
Excluded volume excluded_volume60601 ų
Envelope volume envelope_volume72000 ų
Hydration-shell volume shell_volume23478 ų
Envelope diameter envelope_diameter101.8
Shell Rg shell_rg32.45
Envelope Rg envelope_rg27.90
Shape Rg shape_rg27.89
Total Rg total_rg28.34
Total atoms total_atoms3366
Residues n_residues442
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 dmax99.3
Rg (real space) rg_real28.46
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real3.5350e+07
I(0) uncertainty (real space) i0_real_error5.6290e+05
Rg (reciprocal space) rg_reciprocal28.35
I(0) (reciprocal space) i0_reciprocal35350000.0000
Solution quality estimate total_estimate0.7882
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.1
Skewness Skewness skewness0.553
Kurtosis Kurtosis kurtosis-0.368
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15000000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.619; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.479; Smooth: 0.906

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1ejyi_
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_id1ejyI00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant

8. Citations (2)

9. Files and Curves (10)