2q5d

Crystal Structure of Human Importin Beta bound to the Snurportin1 IBB-domain second crystal form

Method: X-RAY DIFFRACTION Dmax: 141.6 Å Quality: GOOD

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

Importin beta-1 subunit

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;285 K;22%PEG 8000, 0.05M SODIUM CHLORIDE 0.1M MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 285K Resolution 3.20 Å R-free 0.328
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–876 Not recorded Snurportin-1 × 1 (O95149) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;285 K;22%PEG 8000, 0.05M SODIUM CHLORIDE 0.1M MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 285K Resolution 3.20 Å R-free 0.328

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 B; 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 C; UniProt 25–64 Fragment:N-terminal domain (25-64) Importin beta-1 subunit × 1 (Q14974) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;285 K;22%PEG 8000, 0.05M SODIUM CHLORIDE 0.1M MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 285K Resolution 3.20 Å R-free 0.328
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 25–64 Fragment:N-terminal domain (25-64) Importin beta-1 subunit × 1 (Q14974) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;285 K;22%PEG 8000, 0.05M SODIUM CHLORIDE 0.1M MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 285K Resolution 3.20 Å R-free 0.328

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 C; 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 2q5d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2q5d
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2q5d
Deposition date deposition_date2007-05-31
Structure title titleCrystal Structure of Human Importin Beta bound to the Snurportin1 IBB-domain second crystal form
Keywords keywordsHEAT REPEAT, IBB-DOMAIN, IMPORTIN, KARYOPHERIN, SNURPORTIN, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier43.19
Radius of gyration Rg (electron density) rg_electron43.11
Forward intensity I(0) i0578559000.00
Molecular weight molecular_weight196210.0 kDa
Excluded volume excluded_volume245460 ų
Envelope volume envelope_volume360890 ų
Hydration-shell volume shell_volume70534 ų
Envelope diameter envelope_diameter150.0
Shell Rg shell_rg47.83
Envelope Rg envelope_rg41.88
Shape Rg shape_rg43.11
Total Rg total_rg43.35
Total atoms total_atoms13750
Residues n_residues1775
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 dmax141.6
Rg (real space) rg_real43.17
Rg uncertainty (real space) rg_real_error1.31
I(0) (real space) i0_real5.7860e+08
I(0) uncertainty (real space) i0_real_error1.0600e+07
Rg (reciprocal space) rg_reciprocal43.19
I(0) (reciprocal space) i0_reciprocal578600000.0000
Solution quality estimate total_estimate0.8583
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary53.6
Skewness Skewness skewness0.368
Kurtosis Kurtosis kurtosis-0.204
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha40000000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.802; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.753

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd2q5da_
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_idd2q5db_
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_idd2q5dc_
Class classg — Small proteins
Fold Fold foldg.88 — Intrinsically disordered proteins
Superfamily Superfamily superfamilyg.88.2 — importin-beta binding (IBB) domain of snurportin-1
Family Family familyg.88.2.1 — importin-beta binding (IBB) domain of snurportin-1
Domain ID domain_idd2q5dd_
Class classg — Small proteins
Fold Fold foldg.88 — Intrinsically disordered proteins
Superfamily Superfamily superfamilyg.88.2 — importin-beta binding (IBB) domain of snurportin-1
Family Family familyg.88.2.1 — importin-beta binding (IBB) domain of snurportin-1

CATH v4.4 (2 domains)

Domain ID domain_id2q5dA00
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_id2q5dB00
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)