Download MendeleyStructural basis for the assembly of a nuclear export complex.
Matsuura, Y., Stewart, M.(2004) Nature 432: 872-877
1WA5
Structure of the Cse1:Imp-alpha:RanGTP complex
- PDB DOI: https://doi.org/10.2210/pdb1WA5/pdb
- Classification: TRANSPORT PROTEIN
- Organism(s): Canis lupus familiaris, Saccharomyces cerevisiae
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2004-10-23 Released: 2004-12-13
- Funding Organization(s): Human Frontier Science Program (HFSP)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.00 ?
- R-Value Free: 0.216
- R-Value Work: 0.188
- R-Value Observed: 0.190
Starting Models: experimental
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This is version 2.1 of the entry. See complete history.
Literature
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| GTP-binding nuclear protein Ran | 176 | Canis lupus familiaris | Mutation(s): 0 Gene Names: RAN EC: 3.6.5 |  | |
UniProt | |||||
Find proteins for P62825 (Canis lupus familiaris) Explore P62825 Go to UniProtKB: P62825 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P62825 | ||||
Sequence AnnotationsExpand | |||||
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Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| SRP1 isoform 1 | 530 | Saccharomyces cerevisiae | Mutation(s): 0 Gene Names: SRP1, GI526_G0004888 |  | |
UniProt | |||||
Find proteins for Q02821 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c)) Explore Q02821 Go to UniProtKB: Q02821 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q02821 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 3 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Importin alpha re-exporter | 960 | Saccharomyces cerevisiae | Mutation(s): 0 Gene Names: CSE1, YGL238W, HRC135 |  | |
UniProt | |||||
Find proteins for P33307 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c)) Explore P33307 Go to UniProtKB: P33307 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P33307 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| GTP Query on GTP | D [auth A] | GUANOSINE-5'-TRIPHOSPHATE C10 H16 N5 O14 P3 XKMLYUALXHKNFT-UUOKFMHZSA-N |  | ||
| MG Query on MG | E [auth A] | MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.00 ?
- R-Value Free: 0.216
- R-Value Work: 0.188
- R-Value Observed: 0.190
- Space Group: C 1 2 1
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 272.672 | ¦Á = 90 |
| b = 72.261 | ¦Â = 92.57 |
| c = 97.64 | ¦Ă = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| PDB_EXTRACT | data extraction |
| MOSFLM | data reduction |
| SCALA | data scaling |
| CNS | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2004-12-13 Deposition Author(s): Stewart, M.
| Funding Organization | Location | Grant Number |
|---|---|---|
| Human Frontier Science Program (HFSP) | -- |
Revision History (Full details and data files)
- Version 1.0: 2004-12-13
Type: Initial release - Version 1.1: 2011-05-08
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Version format compliance - Version 2.0: 2020-11-04
Changes: Advisory, Atomic model, Author supporting evidence, Data collection, Database references, Derived calculations, Experimental preparation, Other, Polymer sequence, Refinement description, Source and taxonomy, Structure summary, Version format compliance - Version 2.1: 2023-12-13
Changes: Data collection, Database references, Refinement description
