5gxw

Importin and NuMA complex

Method: X-RAY DIFFRACTION Dmax: 98.0 Å Quality: REASONABLE

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 A; UniProt 70–497 Fragment:UNP residues 70-497 Peptide from Nuclear mitotic apparatus protein 1 × 1 (Q14980) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;1M KCl, 0.8M ammonium sulfate, 100mM Hepes, pH 7.0 Resolution 2.39 Å R-free 0.218

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 A; PDBConstruct 1–428; UniProt 70–497

Peptide from Nuclear mitotic apparatus protein 1

Homo sapiens

UniProt Q14980

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 1984–2010 Fragment:UNP residues 1984-2010 Importin subunit alpha-1 × 1 (P52293) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;1M KCl, 0.8M ammonium sulfate, 100mM Hepes, pH 7.0 Resolution 2.39 Å R-free 0.218

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.

4 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NUMA1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–27; UniProt 1984–2010

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 5gxw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5gxw
Deposition date deposition_date2016-09-20
Structure title titleImportin and NuMA complex
Keywords keywordsImportin NuMA complex, 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_guinier28.20
Radius of gyration Rg (electron density) rg_electron27.99
Forward intensity I(0) i038291700.00
Molecular weight molecular_weight49392.0 kDa
Excluded volume excluded_volume62354 ų
Envelope volume envelope_volume76037 ų
Hydration-shell volume shell_volume24527 ų
Envelope diameter envelope_diameter101.2
Shell Rg shell_rg32.89
Envelope Rg envelope_rg28.22
Shape Rg shape_rg27.99
Total Rg total_rg28.49
Total atoms total_atoms3476
Residues n_residues455
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 dmax98.0
Rg (real space) rg_real28.58
Rg uncertainty (real space) rg_real_error0.90
I(0) (real space) i0_real3.8290e+07
I(0) uncertainty (real space) i0_real_error5.4310e+05
Rg (reciprocal space) rg_reciprocal28.47
I(0) (reciprocal space) i0_reciprocal38290000.0000
Solution quality estimate total_estimate0.6146
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.5
Skewness Skewness skewness0.569
Kurtosis Kurtosis kurtosis-0.344
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18200000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.636; Stabil: 1.000; Sysdev: 0.242; Positv: 1.000; Valcen: 0.537; Smooth: 0.814

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_idd5gxwa_
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_id5gxwA00
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)