3oqs

Crystal structure of importin-alpha bound to a CLIC4 NLS peptide

Method: X-RAY DIFFRACTION Dmax: 98.9 Å Quality: GOOD

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

peptide of Chloride intracellular channel protein 4

OrganismNot specified

UniProt Q9Y696

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 198–207 Fragment:NLS (Nuclear Localisation Signal) UNP residues 198-207 Importin subunit alpha-2 × 1 (P52293) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;293 K;0.7M sodium citrate, 10mM DTT, 70mM HEPES pH 7.4, vapor diffusion, hanging drop, temperature 293K Resolution 2.00 Å R-free 0.237

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.

2 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CLIC4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–10; UniProt 198–207

Importin subunit alpha-2

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 Fragment:NLS Binding Domain (UNP residues 70-529) peptide of Chloride intracellular channel protein 4 × 1 (Q9Y696) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;293 K;0.7M sodium citrate, 10mM DTT, 70mM HEPES pH 7.4, vapor diffusion, hanging drop, temperature 293K Resolution 2.00 Å R-free 0.237

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 A; PDBConstruct 51–510; 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 3oqs

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3oqs
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3oqs
Deposition date deposition_date2010-09-03
Structure title titleCrystal structure of importin-alpha bound to a CLIC4 NLS peptide
Keywords keywords;importin alpha, karyopherin alpha, nuclear localisation signal (NLS) recognition, chloride intracellular channel 4, CLIC4 NLS, Armadillo repeat, Nuclear import, 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_guinier28.35
Radius of gyration Rg (electron density) rg_electron28.08
Forward intensity I(0) i033946500.00
Molecular weight molecular_weight46869.0 kDa
Excluded volume excluded_volume59368 ų
Envelope volume envelope_volume71969 ų
Hydration-shell volume shell_volume22944 ų
Envelope diameter envelope_diameter102.2
Shell Rg shell_rg33.00
Envelope Rg envelope_rg28.05
Shape Rg shape_rg28.08
Total Rg total_rg28.59
Total atoms total_atoms3300
Residues n_residues432
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 dmax98.9
Rg (real space) rg_real28.71
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real3.3950e+07
I(0) uncertainty (real space) i0_real_error5.7120e+05
Rg (reciprocal space) rg_reciprocal28.60
I(0) (reciprocal space) i0_reciprocal33940000.0000
Solution quality estimate total_estimate0.7962
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.0
Skewness Skewness skewness0.520
Kurtosis Kurtosis kurtosis-0.431
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11170000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.664; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.505; Smooth: 0.851

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_id3oqsA00
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)