4yi0

Structure of mouse importin a1 bound to Pom121NLS

Method: X-RAY DIFFRACTION Dmax: 98.6 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 C; UniProt 70–529 Fragment:unp residues 70-529 Nuclear envelope pore membrane protein POM 121 × 1 (P52591) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;293 K;0.1 M sodium citrate tribasic dihydrate, 0.7 M sodium citrate tribasic dihydrate, 25 mM DTT Resolution 1.81 Å R-free 0.210

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 C; PDBConstruct 1–460; UniProt 70–529

Nuclear envelope pore membrane protein POM 121

Rattus norvegicus

UniProt P52591

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 291–320 Fragment:unp residues 291-320 Importin subunit alpha-1 × 1 (P52293) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;293 K;0.1 M sodium citrate tribasic dihydrate, 0.7 M sodium citrate tribasic dihydrate, 25 mM DTT Resolution 1.81 Å R-free 0.210

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 PO121_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–30; UniProt 291–320

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 4yi0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4yi0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4yi0
Deposition date deposition_date2015-02-27
Structure title titleStructure of mouse importin a1 bound to Pom121NLS
Keywords keywordskaryopherin; Armadillo repeat: complex; NLS, 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_guinier27.97
Radius of gyration Rg (electron density) rg_electron27.83
Forward intensity I(0) i038028300.00
Molecular weight molecular_weight48948.0 kDa
Excluded volume excluded_volume61777 ų
Envelope volume envelope_volume75764 ų
Hydration-shell volume shell_volume24677 ų
Envelope diameter envelope_diameter101.8
Shell Rg shell_rg32.53
Envelope Rg envelope_rg27.92
Shape Rg shape_rg27.83
Total Rg total_rg28.32
Total atoms total_atoms3446
Residues n_residues452
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 dmax98.6
Rg (real space) rg_real28.33
Rg uncertainty (real space) rg_real_error0.94
I(0) (real space) i0_real3.8030e+07
I(0) uncertainty (real space) i0_real_error5.5150e+05
Rg (reciprocal space) rg_reciprocal28.22
I(0) (reciprocal space) i0_reciprocal38030000.0000
Solution quality estimate total_estimate0.7956
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.2
Skewness Skewness skewness0.574
Kurtosis Kurtosis kurtosis-0.306
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18250000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.622; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.588; Smooth: 0.884

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4yi0c_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.1 — Armadillo repeat

CATH v4.4 (1 domains)

Domain ID domain_id4yi0C00
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)