5h43

Structural and mechanistical studies of the nuclear import by Importin-alpha

Method: X-RAY DIFFRACTION Dmax: 101.0 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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 70–497 Fragment:UNP residues 70-497 Histone acetyltransferase KAT8 × 1 (Q9H7Z6) Histone acetyltransferase KAT8 × 1 (Q9H7Z6) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;3%(v/v) Tacsimate pH5.0, 0.1M Sodium citrate tribasic dehydrate pH5.6, 16%(w/v) PEG 3350 Resolution 2.30 Å R-free 0.243

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 21 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 2–429; UniProt 70–497

Histone acetyltransferase KAT8

Homo sapiens

UniProt Q9H7Z6

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 140–149 Chain C; UniProt 128–142 Fragment:UNP residues 140-149 Fragment:UNP residues 128-142 Importin subunit alpha-1 × 1 (P52292) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;3%(v/v) Tacsimate pH5.0, 0.1M Sodium citrate tribasic dehydrate pH5.6, 16%(w/v) PEG 3350 Resolution 2.30 Å R-free 0.243

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.

41 other PDB entries and 44 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KAT8_HUMAN
Isoform
PDB entities 2, 3
Chains and sequence ranges Author chain B; PDBConstruct 1–10; UniProt 140–149 Author chain C; PDBConstruct 1–15; UniProt 128–142

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 5h43

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5h43
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5h43
Deposition date deposition_date2016-10-28
Structure title titleStructural and mechanistical studies of the nuclear import by Importin-alpha
Keywords keywordsimportin alpha, nuclear import, PROTEIN TRANSPORT-TRANSFERASE complex; PROTEIN TRANSPORT/TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.43
Radius of gyration Rg (electron density) rg_electron28.22
Forward intensity I(0) i038220100.00
Molecular weight molecular_weight49279.0 kDa
Excluded volume excluded_volume62182 ų
Envelope volume envelope_volume75953 ų
Hydration-shell volume shell_volume24225 ų
Envelope diameter envelope_diameter104.5
Shell Rg shell_rg33.07
Envelope Rg envelope_rg28.49
Shape Rg shape_rg28.23
Total Rg total_rg28.69
Total atoms total_atoms3468
Residues n_residues453
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 dmax101.0
Rg (real space) rg_real28.84
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real3.8220e+07
I(0) uncertainty (real space) i0_real_error6.2890e+05
Rg (reciprocal space) rg_reciprocal28.72
I(0) (reciprocal space) i0_reciprocal38220000.0000
Solution quality estimate total_estimate0.7769
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.4
Skewness Skewness skewness0.581
Kurtosis Kurtosis kurtosis-0.315
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha20970000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.580; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.454; Smooth: 0.901

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd5h43a_
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_id5h43A00
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)