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5xah

Crystal structure of human Importin4

Method: X-RAY DIFFRACTION Dmax: 139.1 Å Quality: REASONABLE
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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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 668–1081 Fragment：UNP residues 668-1081 Non-standard monomer：Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；291 K；Sodium Tartrate, PEG3350 Resolution 3.00 Å R-free 0.280
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain B； UniProt 668–1081 Fragment：UNP residues 668-1081 Non-standard monomer：Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；291 K；Sodium Tartrate, PEG3350 Resolution 3.00 Å R-free 0.280
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain C； UniProt 668–1081 Fragment：UNP residues 668-1081 Non-standard monomer：Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；291 K；Sodium Tartrate, PEG3350 Resolution 3.00 Å R-free 0.280
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain D； UniProt 668–1081 Fragment：UNP residues 668-1081 Non-standard monomer：Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；291 K；Sodium Tartrate, PEG3350 Resolution 3.00 Å R-free 0.280

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.

Other PDB Difference from Current Entry 5XAH Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
5XBK Crystal structure of human Importin4 Deposited 2017-03-20 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 668–1081（414 aa） Fragment：UNP residues 668-1081
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；Sodium tartrate, PEG3350
Resolution 3.22 Å R-free 0.281
5XBK Crystal structure of human Importin4 Deposited 2017-03-20 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 668–1081（414 aa） Fragment：UNP residues 668-1081
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；Sodium tartrate, PEG3350
Resolution 3.22 Å R-free 0.281
5XBK Crystal structure of human Importin4 Deposited 2017-03-20 Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 668–1081（414 aa） Fragment：UNP residues 668-1081
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；Sodium tartrate, PEG3350
Resolution 3.22 Å R-free 0.281
5XBK Crystal structure of human Importin4 Deposited 2017-03-20 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 668–1081（414 aa） Fragment：UNP residues 668-1081
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；Sodium tartrate, PEG3350
Resolution 3.22 Å R-free 0.281
7UNK Structure of Importin-4 bound to the H3-H4-ASF1 histone-histone chaperone complex Deposited 2022-04-11 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–1081（1081 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.45 Å
8DYO Cryo-EM structure of Importin-4 bound to RanGTP Deposited 2022-08-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–1081（1081 aa）
Not recorded 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

3 other PDB entries and 6 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 3–416； UniProt 668–1081 Author chain B； PDBConstruct 3–416； UniProt 668–1081 Author chain C； PDBConstruct 3–416； UniProt 668–1081 Author chain D； PDBConstruct 3–416； UniProt 668–1081

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 5xah

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5xah
Deposition date deposition_date2017-03-13
Structure title titleCrystal structure of human Importin4
Keywords keywordsHistone, Chromatin, Assembly, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier42.50 Å
Radius of gyration Rg (electron density) rg_electron42.37 Å
Forward intensity I(0) i0376958000.00
Molecular weight molecular_weight161470.0 kDa
Excluded volume excluded_volume203250 ų
Envelope volume envelope_volume282860 ų
Hydration-shell volume shell_volume58090 ų
Envelope diameter envelope_diameter148.5 Å
Shell Rg shell_rg45.43 Å
Envelope Rg envelope_rg41.38 Å
Shape Rg shape_rg42.37 Å
Total Rg total_rg42.53 Å
Total atoms total_atoms11255
Residues n_residues1467
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax139.1 Å
Rg (real space) rg_real42.55 Å
Rg uncertainty (real space) rg_real_error1.15 Å
I(0) (real space) i0_real3.7700e+08
I(0) uncertainty (real space) i0_real_error6.7780e+06
Rg (reciprocal space) rg_reciprocal42.50 Å
I(0) (reciprocal space) i0_reciprocal376900000.0000
Solution quality estimate total_estimate0.6453
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.9 Å
Skewness Skewness skewness0.365
Kurtosis Kurtosis kurtosis-0.385
Angular range angular_range— – 0.1850 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19430000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.844; Stabil: 1.000; Sysdev: 0.016; Positv: 1.000; Valcen: 1.000; Smooth: 0.805
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (2)

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9. Files and Curves (10)