3lww

Structure of an open and closed conformation of Human Importin Beta bound to the Snurportin1 IBB-domain trapped in the same crystallographic asymmetric unit

Method: X-RAY DIFFRACTION Dmax: 141.0 Å Quality: GOOD

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

Importin subunit beta-1

Homo sapiens

UniProt Q14974

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 1–876 Not recorded Snurportin-1 × 1 (O95149) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;18% PEG 8000, 50 mM sodium chloride, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 3.15 Å R-free 0.313
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–876 Not recorded Snurportin-1 × 1 (O95149) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;18% PEG 8000, 50 mM sodium chloride, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 3.15 Å R-free 0.313

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.

22 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IMB1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–876; UniProt 1–876 Author chain C; PDBConstruct 1–876; UniProt 1–876

Snurportin-1

OrganismNot specified

UniProt O95149

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 25–64 Fragment:Snurportin1 N-terminal domain (25-64) Importin subunit beta-1 × 1 (Q14974) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;18% PEG 8000, 50 mM sodium chloride, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 3.15 Å R-free 0.313
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 25–64 Fragment:Snurportin1 N-terminal domain (25-64) Importin subunit beta-1 × 1 (Q14974) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;18% PEG 8000, 50 mM sodium chloride, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 3.15 Å R-free 0.313

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.

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

View Construct and Data Evidence
UniProt name SPN1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–40; UniProt 25–64 Author chain D; PDBConstruct 1–40; UniProt 25–64

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 3lww

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3lww
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3lww
Deposition date deposition_date2010-02-24
Structure title titleStructure of an open and closed conformation of Human Importin Beta bound to the Snurportin1 IBB-domain trapped in the same crystallographic asymmetric unit
Keywords keywordsPROTEIN TRANSPORT, HEAT repeat, IBB-domain, Importin beta, Karyopherin, Snurportin; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier42.62
Radius of gyration Rg (electron density) rg_electron42.47
Forward intensity I(0) i0609122000.00
Molecular weight molecular_weight201580.0 kDa
Excluded volume excluded_volume252130 ų
Envelope volume envelope_volume351410 ų
Hydration-shell volume shell_volume69383 ų
Envelope diameter envelope_diameter144.0
Shell Rg shell_rg47.69
Envelope Rg envelope_rg41.27
Shape Rg shape_rg42.48
Total Rg total_rg42.72
Total atoms total_atoms14127
Residues n_residues1809
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 dmax141.0
Rg (real space) rg_real42.59
Rg uncertainty (real space) rg_real_error1.64
I(0) (real space) i0_real6.0910e+08
I(0) uncertainty (real space) i0_real_error1.0920e+07
Rg (reciprocal space) rg_reciprocal42.62
I(0) (reciprocal space) i0_reciprocal609100000.0000
Solution quality estimate total_estimate0.8766
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary49.5
Skewness Skewness skewness0.331
Kurtosis Kurtosis kurtosis-0.370
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha41530000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.843; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.865

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3lwwa_
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
Domain ID domain_idd3lwwc_
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 (2 domains)

Domain ID domain_id3lwwA00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant
Domain ID domain_id3lwwC00
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)