7leq

Structure of importin a2 bound to p50 NLS

Method: X-RAY DIFFRACTION Dmax: 99.7 Å Quality: GOOD

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

Importin subunit alpha-1

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 E; UniProt 70–497 Not recorded Nuclear factor NF-kappa-B p105 subunit × 1 (P19838) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;0.6M sodium citrate, 100 Hepes pH 6.0 Resolution 2.24 Å R-free 0.219

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 IMA1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain E; PDBConstruct 1–428; UniProt 70–497

Nuclear factor NF-kappa-B p105 subunit

OrganismNot specified

UniProt P19838

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 355–368 Fragment:Nuclear localization signal motif, residues 355-368 Importin subunit alpha-1 × 1 (P52293) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;0.6M sodium citrate, 100 Hepes pH 6.0 Resolution 2.24 Å R-free 0.219

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.

13 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NFKB1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–14; UniProt 355–368

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 7leq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7leq
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7leq
Deposition date deposition_date2021-01-14
Structure title titleStructure of importin a2 bound to p50 NLS
Keywords keywordsNUCLEAR IMPORT, IMPORTIN ALPHA, NLS, NF-kB, p50, 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_guinier28.29
Radius of gyration Rg (electron density) rg_electron28.02
Forward intensity I(0) i033693500.00
Molecular weight molecular_weight46554.0 kDa
Excluded volume excluded_volume58928 ų
Envelope volume envelope_volume72526 ų
Hydration-shell volume shell_volume23132 ų
Envelope diameter envelope_diameter102.1
Shell Rg shell_rg33.01
Envelope Rg envelope_rg28.14
Shape Rg shape_rg28.02
Total Rg total_rg28.55
Total atoms total_atoms3276
Residues n_residues430
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 dmax99.7
Rg (real space) rg_real28.65
Rg uncertainty (real space) rg_real_error0.98
I(0) (real space) i0_real3.3690e+07
I(0) uncertainty (real space) i0_real_error5.5360e+05
Rg (reciprocal space) rg_reciprocal28.54
I(0) (reciprocal space) i0_reciprocal33690000.0000
Solution quality estimate total_estimate0.7948
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.1
Skewness Skewness skewness0.531
Kurtosis Kurtosis kurtosis-0.400
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11680000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.643; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.491; Smooth: 0.908

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id7leqE01
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)