3wpt

Crystal structure of closed dimer of human importin-alpha1 (Rch1)

Method: X-RAY DIFFRACTION Dmax: 100.5 Å Quality: GOOD

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

Importin subunit alpha-1

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 75–497 Fragment:UNP residues 75-497 PEG DI(HYDROXYETHYL)ETHER × 11 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;50MM MES, 100MM AMMONIUM SULFATE, 10MM MGCL, 15-20%(w/v) PEG8000, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.63 Å R-free 0.216
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 75–497 Fragment:UNP residues 75-497 PEG DI(HYDROXYETHYL)ETHER × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;50MM MES, 100MM AMMONIUM SULFATE, 10MM MGCL, 15-20%(w/v) PEG8000, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.63 Å R-free 0.216

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 IMA1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–423; UniProt 75–497 Author chain B; PDBConstruct 1–423; UniProt 75–497

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 3wpt

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3wpt
Deposition date deposition_date2014-01-17
Structure title titleCrystal structure of closed dimer of human importin-alpha1 (Rch1)
Keywords keywords;Arm repeat, All Alpha protein, Armadillo repeat, Closed dimer, Nuclear transport, importin-beta, NLS-carring proteins, 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_guinier30.71
Radius of gyration Rg (electron density) rg_electron30.02
Forward intensity I(0) i0128232000.00
Molecular weight molecular_weight93128.0 kDa
Excluded volume excluded_volume118080 ų
Envelope volume envelope_volume144510 ų
Hydration-shell volume shell_volume40535 ų
Envelope diameter envelope_diameter104.0
Shell Rg shell_rg37.09
Envelope Rg envelope_rg29.73
Shape Rg shape_rg30.03
Total Rg total_rg30.64
Total atoms total_atoms13292
Residues n_residues845
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 dmax100.5
Rg (real space) rg_real30.75
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real1.2820e+08
I(0) uncertainty (real space) i0_real_error1.7340e+06
Rg (reciprocal space) rg_reciprocal30.73
I(0) (reciprocal space) i0_reciprocal128200000.0000
Solution quality estimate total_estimate0.8766
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary34.8
Skewness Skewness skewness0.426
Kurtosis Kurtosis kurtosis-0.228
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha32950000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.849; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.851

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3wpta_
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_idd3wptb_
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 (2 domains)

Domain ID domain_id3wptA00
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_id3wptB00
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)