1wa5

Structure of the Cse1:Imp-alpha:RanGTP complex

Method: X-RAY DIFFRACTION Dmax: 131.7 Å Quality: GOOD

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

GTP-binding nuclear protein Ran

Canis lupus familiaris

UniProt P62825

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 1–176 Not recorded SRP1 isoform 1 × 1 (A0A6A5Q590) Importin alpha re-exporter × 1 (P33307) GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.6;291 K;50mM TrisHCl, 200mM NaCl, 5mM Mg(OAc)2, .1mM GTP, 22% PEG3350 and 2% PEG400. Resolution 2.00 Å R-free 0.216

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.

9 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAN_CANLF
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–176; UniProt 1–176

SRP1 isoform 1

Saccharomyces cerevisiae

UniProt A0A6A5Q590

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 1–530 Not recorded GTP-binding nuclear protein Ran × 1 (P62825) Importin alpha re-exporter × 1 (P33307) GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.6;291 K;50mM TrisHCl, 200mM NaCl, 5mM Mg(OAc)2, .1mM GTP, 22% PEG3350 and 2% PEG400. Resolution 2.00 Å R-free 0.216

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 A0A6A5Q590_YEASX
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–530; UniProt 1–530

Importin alpha re-exporter

Saccharomyces cerevisiae

UniProt P33307

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 C; UniProt 1–960 Not recorded GTP-binding nuclear protein Ran × 1 (P62825) SRP1 isoform 1 × 1 (A0A6A5Q590) GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.6;291 K;50mM TrisHCl, 200mM NaCl, 5mM Mg(OAc)2, .1mM GTP, 22% PEG3350 and 2% PEG400. Resolution 2.00 Å R-free 0.216

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.

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CSE1_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–960; UniProt 1–960

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 1wa5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1wa5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1wa5
Deposition date deposition_date2004-10-23
Structure title titleStructure of the Cse1:Imp-alpha:RanGTP complex
Keywords keywordsCse1, Importin-alpha, RanGTP, nuclear 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_guinier39.57
Radius of gyration Rg (electron density) rg_electron39.17
Forward intensity I(0) i0451358000.00
Molecular weight molecular_weight180460.0 kDa
Excluded volume excluded_volume229040 ų
Envelope volume envelope_volume293740 ų
Hydration-shell volume shell_volume62715 ų
Envelope diameter envelope_diameter139.2
Shell Rg shell_rg45.05
Envelope Rg envelope_rg38.63
Shape Rg shape_rg39.15
Total Rg total_rg39.59
Total atoms total_atoms25639
Residues n_residues1586
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 dmax131.7
Rg (real space) rg_real39.54
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real4.5140e+08
I(0) uncertainty (real space) i0_real_error7.5530e+06
Rg (reciprocal space) rg_reciprocal39.56
I(0) (reciprocal space) i0_reciprocal451400000.0000
Solution quality estimate total_estimate0.8747
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary49.4
Skewness Skewness skewness0.354
Kurtosis Kurtosis kurtosis-0.170
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha69740000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.851; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.814

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1wa5a_
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_idd1wa5b_
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_idd1wa5c_
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 (3 domains)

Domain ID domain_id1wa5A00
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_id1wa5B00
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_id1wa5C00
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)