5w4g

Importin binding to NLS peptide of DNA polymerase lambda

Method: X-RAY DIFFRACTION Dmax: 97.4 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 B; UniProt 70–529 Not recorded DNA polymerase lambda × 1 (Q9UGP5) SO4 SULFATE ION × 4 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;0.1 M Bis Tris Propane 1.4 M Ammonium Sulfate Resolution 2.04 Å R-free 0.200

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 B; PDBConstruct 51–510; UniProt 70–529

DNA polymerase lambda

OrganismNot specified

UniProt Q9UGP5

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 4–32 Not recorded Importin subunit alpha-1 × 1 (P52293) SO4 SULFATE ION × 4 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;0.1 M Bis Tris Propane 1.4 M Ammonium Sulfate Resolution 2.04 Å R-free 0.200

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.

95 other PDB entries and 142 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPOLL_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–29; UniProt 4–32

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 5w4g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5w4g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5w4g
Deposition date deposition_date2017-06-10
Structure title titleImportin binding to NLS peptide of DNA polymerase lambda
Keywords keywordsimportin, NLS, polymerase lambda, Nuclear Transport, Protein Binding; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.65
Radius of gyration Rg (electron density) rg_electron27.35
Forward intensity I(0) i034213700.00
Molecular weight molecular_weight46363.0 kDa
Excluded volume excluded_volume58375 ų
Envelope volume envelope_volume67842 ų
Hydration-shell volume shell_volume22357 ų
Envelope diameter envelope_diameter98.6
Shell Rg shell_rg32.34
Envelope Rg envelope_rg27.39
Shape Rg shape_rg27.35
Total Rg total_rg27.84
Total atoms total_atoms3260
Residues n_residues438
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 dmax97.4
Rg (real space) rg_real27.99
Rg uncertainty (real space) rg_real_error0.78
I(0) (real space) i0_real3.4210e+07
I(0) uncertainty (real space) i0_real_error4.7800e+05
Rg (reciprocal space) rg_reciprocal27.89
I(0) (reciprocal space) i0_reciprocal34210000.0000
Solution quality estimate total_estimate0.7979
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.9
Skewness Skewness skewness0.538
Kurtosis Kurtosis kurtosis-0.398
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11250000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.633; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.544; Smooth: 0.927

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id5w4gB00
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)