9ovz

Gallid alphaherpesvirus-2 large tegument protein NLS in complex with Importin alpha

Method: X-RAY DIFFRACTION Dmax: 98.3 Å Quality: GOOD

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 70–529 Fragment:UNP residues 70-529 Large tegument protein deneddylase × 2 (Q9E6N3) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;296 K;0.7 M sodium citrate, 0.1 M HEPES, 0.01 M DTT, pH 7.0 Resolution 2.40 Å R-free 0.225

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 51–510; UniProt 70–529

Large tegument protein deneddylase

OrganismNot specified

UniProt Q9E6N3

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 467–476 Chain C; UniProt 467–476 Not recorded Importin subunit alpha-1 × 1 (P52293) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;296 K;0.7 M sodium citrate, 0.1 M HEPES, 0.01 M DTT, pH 7.0 Resolution 2.40 Å R-free 0.225

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name LTP_GAHVM
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–10; UniProt 467–476 Author chain C; PDBConstruct 1–10; UniProt 467–476

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 9ovz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ovz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9ovz
Deposition date deposition_date2025-06-02
最后修订 last_revision2026-04-29
Structure title titleGallid alphaherpesvirus-2 large tegument protein NLS in complex with Importin alpha
Keywords keywordsnuclear import, viral protein, transport, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.97
Radius of gyration Rg (electron density) rg_electron27.78
Forward intensity I(0) i035248000.00
Molecular weight molecular_weight47478.0 kDa
Excluded volume excluded_volume60055 ų
Envelope volume envelope_volume72155 ų
Hydration-shell volume shell_volume23232 ų
Envelope diameter envelope_diameter101.7
Shell Rg shell_rg32.82
Envelope Rg envelope_rg27.84
Shape Rg shape_rg27.77
Total Rg total_rg28.32
Total atoms total_atoms3342
Residues n_residues434
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 dmax98.3
Rg (real space) rg_real28.32
Rg uncertainty (real space) rg_real_error1.01
I(0) (real space) i0_real3.5250e+07
I(0) uncertainty (real space) i0_real_error5.8830e+05
Rg (reciprocal space) rg_reciprocal28.22
I(0) (reciprocal space) i0_reciprocal35250000.0000
Solution quality estimate total_estimate0.7969
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.1
Skewness Skewness skewness0.541
Kurtosis Kurtosis kurtosis-0.382
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14330000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.630; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.555; Smooth: 0.910

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)