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1z3h

The exportin Cse1 in its cargo-free, cytoplasmic state

Method: X-RAY DIFFRACTION Dmax: 179.2 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–960 Not recorded MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；PEG 8000, MgCl2, glycerol, DTT, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.10 Å R-free 0.288
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain B； UniProt 1–960 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；PEG 8000, MgCl2, glycerol, DTT, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.10 Å R-free 0.288

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.

Other PDB Difference from Current Entry 1Z3H Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1WA5 Structure of the Cse1:Imp-alpha:RanGTP complex Deposited 2004-10-23 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 1–960（960 aa）
Not recorded 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

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

View Construct and Data Evidence
UniProt name CSE1_YEAST
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–960； UniProt 1–960 Author chain B； 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 1z3h

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1z3h
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1z3h
Deposition date deposition_date2005-03-12
Structure title titleThe exportin Cse1 in its cargo-free, cytoplasmic state
Keywords keywordsCse1, Exportin, Nuclear transport, HEAT repeat, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier50.84 Å
Radius of gyration Rg (electron density) rg_electron51.02 Å
Forward intensity I(0) i0561498000.00
Molecular weight molecular_weight209350.0 kDa
Excluded volume excluded_volume267620 ų
Envelope volume envelope_volume384260 ų
Hydration-shell volume shell_volume66418 ų
Envelope diameter envelope_diameter182.3 Å
Shell Rg shell_rg50.41 Å
Envelope Rg envelope_rg49.60 Å
Shape Rg shape_rg51.01 Å
Total Rg total_rg51.04 Å
Total atoms total_atoms14787
Residues n_residues1839
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax179.2 Å
Rg (real space) rg_real51.12 Å
Rg uncertainty (real space) rg_real_error1.98 Å
I(0) (real space) i0_real5.6150e+08
I(0) uncertainty (real space) i0_real_error1.1200e+07
Rg (reciprocal space) rg_reciprocal50.61 Å
I(0) (reciprocal space) i0_reciprocal561100000.0000
Solution quality estimate total_estimate0.8255
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary57.8 Å
Skewness Skewness skewness0.526
Kurtosis Kurtosis kurtosis-0.207
Angular range angular_range— – 0.1550 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha27800000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.737; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.899; Smooth: 0.619
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1z3ha1
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_idd1z3hb_
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
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8. Citations (1)

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9. Files and Curves (10)