4e4v

The crystal structure of the dimeric human importin alpha 1 at 2.5 angstrom resolution.

Method: X-RAY DIFFRACTION Dmax: 101.2 Å Quality: GOOD

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

Importin subunit alpha-2

Homo sapiens

UniProt P52292

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 70–529 Fragment:Importin alpha 1 lacking IBB domain (UNP residues 70-529) Mutation:K486R GOL GLYCEROL × 8 DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.4;298 K;0.5 CITRATE PH 5.4 10 MM DTT, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.53 Å R-free 0.203
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 70–529 Fragment:Importin alpha 1 lacking IBB domain (UNP residues 70-529) Mutation:K486R GOL GLYCEROL × 5 DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.4;298 K;0.5 CITRATE PH 5.4 10 MM DTT, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.53 Å R-free 0.203

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 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IMA2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 26–485; UniProt 70–529 Author chain B; PDBConstruct 26–485; 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 4e4v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4e4v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4e4v
Deposition date deposition_date2012-03-13
Structure title titleThe crystal structure of the dimeric human importin alpha 1 at 2.5 angstrom resolution.
Keywords keywords;armadillo repeat, karyopherin, importin, nuclear import, host-virus interaction, nucleus, phosphoprotein, protein transport, transport, 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_guinier31.15
Radius of gyration Rg (electron density) rg_electron30.45
Forward intensity I(0) i0135265000.00
Molecular weight molecular_weight95057.0 kDa
Excluded volume excluded_volume120190 ų
Envelope volume envelope_volume145570 ų
Hydration-shell volume shell_volume40467 ų
Envelope diameter envelope_diameter105.8
Shell Rg shell_rg37.32
Envelope Rg envelope_rg29.97
Shape Rg shape_rg30.43
Total Rg total_rg31.11
Total atoms total_atoms13513
Residues n_residues866
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 dmax101.2
Rg (real space) rg_real31.20
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real1.3530e+08
I(0) uncertainty (real space) i0_real_error1.8000e+06
Rg (reciprocal space) rg_reciprocal31.18
I(0) (reciprocal space) i0_reciprocal135300000.0000
Solution quality estimate total_estimate0.8798
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary35.7
Skewness Skewness skewness0.414
Kurtosis Kurtosis kurtosis-0.301
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha33790000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.873; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.833

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd4e4va1
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
Domain ID domain_idd4e4va2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4e4vb1
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
Domain ID domain_idd4e4vb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id4e4vA00
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_id4e4vB00
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)