3ea5

Kap95p Binding Induces the Switch Loops of RanGDP to adopt the GTP-bound Conformation: Implications for Nuclear Import Complex Assembly Dynamics

Method: X-RAY DIFFRACTION Dmax: 126.8 Å Quality: EXCELLENT

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

GTP-binding nuclear protein Ran

Homo sapiens

UniProt P62826

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 1–216 Mutation:A181C, L254K Importin subunit beta-1 × 1 (Q06142) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.1;298 K;17% PEG 4000 0.1 M MES (pH 6.1) 10 mM MgCl2 125 mM NaCl 12% MPD 5 mg/ml GDP, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.50 Å R-free 0.232
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–216 Mutation:A181C, L254K Importin subunit beta-1 × 1 (Q06142) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.1;298 K;17% PEG 4000 0.1 M MES (pH 6.1) 10 mM MgCl2 125 mM NaCl 12% MPD 5 mg/ml GDP, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.50 Å R-free 0.232

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.

137 other PDB entries and 202 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAN_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–216; UniProt 1–216 Author chain C; PDBConstruct 1–216; UniProt 1–216

Importin subunit beta-1

Saccharomyces cerevisiae

UniProt Q06142

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 1–861 Not recorded GTP-binding nuclear protein Ran × 1 (P62826) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.1;298 K;17% PEG 4000 0.1 M MES (pH 6.1) 10 mM MgCl2 125 mM NaCl 12% MPD 5 mg/ml GDP, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.50 Å R-free 0.232
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–861 Not recorded GTP-binding nuclear protein Ran × 1 (P62826) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.1;298 K;17% PEG 4000 0.1 M MES (pH 6.1) 10 mM MgCl2 125 mM NaCl 12% MPD 5 mg/ml GDP, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.50 Å R-free 0.232

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 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IMB1_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–861; UniProt 1–861 Author chain D; PDBConstruct 1–861; UniProt 1–861

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 3ea5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3ea5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3ea5
Deposition date deposition_date2008-08-24
Structure title titleKap95p Binding Induces the Switch Loops of RanGDP to adopt the GTP-bound Conformation: Implications for Nuclear Import Complex Assembly Dynamics
Keywords keywords;Karyopherin, Importin, Ran, GTP-binding, Host-virus interaction, Nucleotide-binding, Nucleus, Phosphoprotein, Protein transport, Transport, 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_guinier42.59
Radius of gyration Rg (electron density) rg_electron41.84
Forward intensity I(0) i0758249000.00
Molecular weight molecular_weight228550.0 kDa
Excluded volume excluded_volume286860 ų
Envelope volume envelope_volume404510 ų
Hydration-shell volume shell_volume77966 ų
Envelope diameter envelope_diameter127.0
Shell Rg shell_rg50.47
Envelope Rg envelope_rg39.76
Shape Rg shape_rg41.84
Total Rg total_rg42.27
Total atoms total_atoms16064
Residues n_residues2051
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 dmax126.8
Rg (real space) rg_real42.28
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real7.5830e+08
I(0) uncertainty (real space) i0_real_error1.2920e+07
Rg (reciprocal space) rg_reciprocal42.59
I(0) (reciprocal space) i0_reciprocal758500000.0000
Solution quality estimate total_estimate0.9026
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary61.7
Skewness Skewness skewness-0.079
Kurtosis Kurtosis kurtosis-0.688
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha89680000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.936; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.951

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd3ea5a_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins
Domain ID domain_idd3ea5b_
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_idd3ea5c_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins
Domain ID domain_idd3ea5d_
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 (4 domains)

Domain ID domain_id3ea5A00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id3ea5B00
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_id3ea5C00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id3ea5D00
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)