8g8s

bipartite p52 NLS in complex with Importin alpha 2

Method: X-RAY DIFFRACTION Dmax: 98.1 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 A; UniProt 70–529 Not recorded Nuclear factor NF-kappa-B p100 subunit isoform X1 × 1 (F1S861) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;295 K;0.01M DTT, 0.1M sodium HEPES pH7, 0.6M sodium citrate Resolution 2.10 Å R-free 0.186

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 A; PDBConstruct 51–510; UniProt 70–529

Nuclear factor NF-kappa-B p100 subunit isoform X1

Homo sapiens

UniProt F1S861

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 310–344 Not recorded Importin subunit alpha-1 × 1 (P52293) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;295 K;0.01M DTT, 0.1M sodium HEPES pH7, 0.6M sodium citrate Resolution 2.10 Å R-free 0.186

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 F1S861_PIG
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–35; UniProt 310–344

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 8g8s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8g8s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8g8s
Deposition date deposition_date2023-02-19
最后修订 last_revision2024-02-21
Structure title titlebipartite p52 NLS in complex with Importin alpha 2
Keywords keywordsNuclear import, transcription factors, Nf-kB, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.90
Radius of gyration Rg (electron density) rg_electron27.66
Forward intensity I(0) i036353100.00
Molecular weight molecular_weight48290.0 kDa
Excluded volume excluded_volume61104 ų
Envelope volume envelope_volume73069 ų
Hydration-shell volume shell_volume23560 ų
Envelope diameter envelope_diameter101.2
Shell Rg shell_rg32.78
Envelope Rg envelope_rg27.96
Shape Rg shape_rg27.66
Total Rg total_rg28.17
Total atoms total_atoms6896
Residues n_residues443
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_real28.26
Rg uncertainty (real space) rg_real_error1.01
I(0) (real space) i0_real3.6350e+07
I(0) uncertainty (real space) i0_real_error5.4010e+05
Rg (reciprocal space) rg_reciprocal28.15
I(0) (reciprocal space) i0_reciprocal36350000.0000
Solution quality estimate total_estimate0.7957
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.1
Skewness Skewness skewness0.552
Kurtosis Kurtosis kurtosis-0.363
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15360000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.626; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.553; Smooth: 0.909

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)