8dyo

Cryo-EM structure of Importin-4 bound to RanGTP

Method: ELECTRON MICROSCOPY Dmax: 130.1 Å Quality: GOOD

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

Importin-4

Homo sapiens

UniProt Q8TEX9

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 1–1081 Not recorded GTP-binding nuclear protein GSP1/CNR1 × 1 (P32835) MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.10 Å

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.

3 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IPO4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1081; UniProt 1–1081

GTP-binding nuclear protein GSP1/CNR1

Saccharomyces cerevisiae

UniProt P32835

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 1–219 Not recorded Importin-4 × 1 (Q8TEX9) MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.10 Å

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.

11 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GSP1_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–219; UniProt 1–219

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 8dyo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8dyo
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8dyo
Deposition date deposition_date2022-08-04
Structure title titleCryo-EM structure of Importin-4 bound to RanGTP
Keywords keywordsImportin, Karyopherin, GTPase, nuclear import, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.08
Radius of gyration Rg (electron density) rg_electron39.09
Forward intensity I(0) i0253820000.00
Molecular weight molecular_weight131210.0 kDa
Excluded volume excluded_volume165690 ų
Envelope volume envelope_volume249490 ų
Hydration-shell volume shell_volume54461 ų
Envelope diameter envelope_diameter139.9
Shell Rg shell_rg43.98
Envelope Rg envelope_rg37.89
Shape Rg shape_rg39.11
Total Rg total_rg39.39
Total atoms total_atoms9212
Residues n_residues1187
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 dmax130.1
Rg (real space) rg_real39.09
Rg uncertainty (real space) rg_real_error1.16
I(0) (real space) i0_real2.5380e+08
I(0) uncertainty (real space) i0_real_error4.8720e+06
Rg (reciprocal space) rg_reciprocal39.09
I(0) (reciprocal space) i0_reciprocal253800000.0000
Solution quality estimate total_estimate0.8770
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.8
Skewness Skewness skewness0.350
Kurtosis Kurtosis kurtosis-0.220
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25090000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.871; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.787

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)