8hkw

Crystal structure of importin-alpha3 bound to the 53BP1 nuclear localization signal

Method: X-RAY DIFFRACTION Dmax: 98.3 Å Quality: GOOD

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

Importin subunit alpha-3

Homo sapiens

UniProt O00629

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 70–485 Chain B; UniProt 70–485 Fragment:UNP residues 70-485 Peptide from TP53-binding protein 1 × 2 (Q12888) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Mother liquor contained PEG3350 and lithium nitrate. Crystal was grown in the presence of a synthetic peptide (amino acid sequence: GTSFSGRKIKTAVRRRK) that corresponds to human Nup153 residues 1459-1475). Resolution 1.90 Å R-free 0.221

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.

16 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IMA3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–416; UniProt 70–485 Author chain B; PDBConstruct 1–416; UniProt 70–485

Peptide from TP53-binding protein 1

Homo sapiens

UniProt Q12888

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1665–1686 Chain D; UniProt 1665–1686 Not recorded Importin subunit alpha-3 × 2 (O00629) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Mother liquor contained PEG3350 and lithium nitrate. Crystal was grown in the presence of a synthetic peptide (amino acid sequence: GTSFSGRKIKTAVRRRK) that corresponds to human Nup153 residues 1459-1475). Resolution 1.90 Å R-free 0.221

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.

34 other PDB entries and 68 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TP53B_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–22; UniProt 1665–1686 Author chain D; PDBConstruct 1–22; UniProt 1665–1686

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 8hkw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8hkw
Deposition date deposition_date2022-11-28
Structure title titleCrystal structure of importin-alpha3 bound to the 53BP1 nuclear localization signal
Keywords keywordsimportin alpha, nuclear localization signal, nuclear import, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.24
Radius of gyration Rg (electron density) rg_electron29.20
Forward intensity I(0) i0142928000.00
Molecular weight molecular_weight95946.0 kDa
Excluded volume excluded_volume120770 ų
Envelope volume envelope_volume148580 ų
Hydration-shell volume shell_volume41940 ų
Envelope diameter envelope_diameter103.1
Shell Rg shell_rg36.90
Envelope Rg envelope_rg28.99
Shape Rg shape_rg29.21
Total Rg total_rg29.88
Total atoms total_atoms6750
Residues n_residues872
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 dmax98.3
Rg (real space) rg_real30.11
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real1.4290e+08
I(0) uncertainty (real space) i0_real_error2.0660e+06
Rg (reciprocal space) rg_reciprocal30.17
I(0) (reciprocal space) i0_reciprocal142900000.0000
Solution quality estimate total_estimate0.8828
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.7
Skewness Skewness skewness0.228
Kurtosis Kurtosis kurtosis-0.289
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha102700000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.842; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.949

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id8hkwA01
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_id8hkwB01
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)