6bw1

Hendra virus W protein C-terminus in complex with Importin alpha 1

Method: X-RAY DIFFRACTION Dmax: 99.0 Å Quality: GOOD

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

Protein W

Hendra virus

UniProt P0C1C6

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 C; UniProt 409–448 Not recorded Importin subunit alpha-1 × 1 (P52293) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;0.01M DTT, 0.1M sodium HEPES pH7, 0.7M sodium citrate Resolution 2.20 Å R-free 0.212

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 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name W_HENDH
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 2–41; UniProt 409–448

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 E; UniProt 70–529 Not recorded Protein W × 1 (P0C1C6) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;0.01M DTT, 0.1M sodium HEPES pH7, 0.7M sodium citrate Resolution 2.20 Å R-free 0.212

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 2
Chains and sequence ranges Author chain E; PDBConstruct 51–510; UniProt 70–529

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 6bw1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6bw1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6bw1
Deposition date deposition_date2017-12-14
Structure title titleHendra virus W protein C-terminus in complex with Importin alpha 1
Keywords keywordsComplex, Hendra virus, Importin, Karyopherin, phosphoprotein, W, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.42
Radius of gyration Rg (electron density) rg_electron28.13
Forward intensity I(0) i033946500.00
Molecular weight molecular_weight46957.0 kDa
Excluded volume excluded_volume59495 ų
Envelope volume envelope_volume72816 ų
Hydration-shell volume shell_volume23097 ų
Envelope diameter envelope_diameter102.3
Shell Rg shell_rg33.24
Envelope Rg envelope_rg28.25
Shape Rg shape_rg28.13
Total Rg total_rg28.65
Total atoms total_atoms3306
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 dmax99.0
Rg (real space) rg_real28.79
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real3.3950e+07
I(0) uncertainty (real space) i0_real_error5.0630e+05
Rg (reciprocal space) rg_reciprocal28.68
I(0) (reciprocal space) i0_reciprocal33940000.0000
Solution quality estimate total_estimate0.8008
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary23.0
Skewness Skewness skewness0.524
Kurtosis Kurtosis kurtosis-0.426
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha11580000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.665; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.505; Smooth: 0.906

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_idd6bw1e_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id6bw1E00
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)