Download MendeleyHuman septin 2 in complex with GDP.
Rabeh, W.M., Nedyalkova, L., Tempel, W., Landry, R., Crombet, L., Kozieradzki, I., Senisterra, G., Vedadi, M., Arrowsmith, C.H., Edwards, A.M., Sundstrom, M., Weigelt, J., Bochkarev, A., Park, H.To be published.
2QNR | pdb_00002qnr
Human septin 2 in complex with GDP
- PDB DOI: https://doi.org/10.2210/pdb2QNR/pdb
- Classification: CELL CYCLE
- Organism(s): Homo sapiens
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2007-07-19 Released: 2007-07-31
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.60 Å
- R-Value Free: 0.293 (Depositor), 0.295 (DCC)
- R-Value Work: 0.234 (Depositor), 0.255 (DCC)
wwPDB Validation 3D Report Full Report
This is version 1.3 of the entry. See complete history.
Literature
To be published.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Septin-2 | 301 | Homo sapiens | Mutation(s): 1 Gene Names: SEPT2, DIFF6, KIAA0158, NEDD5 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q15019 (Homo sapiens) Explore Q15019 Go to UniProtKB: Q15019 | |||||
PHAROS: Q15019 GTEx: ENSG00000168385 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q15019 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| GDP Query on GDP | C [auth A], F [auth B] | GUANOSINE-5'-DIPHOSPHATE C10 H15 N5 O11 P2 QGWNDRXFNXRZMB-UUOKFMHZSA-N |  | ||
| UNX Query on UNX | D [auth A], E [auth A], G [auth B], H [auth B] | UNKNOWN ATOM OR ION X |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.60 Å
- R-Value Free: 0.293 (Depositor), 0.295 (DCC)
- R-Value Work: 0.234 (Depositor), 0.255 (DCC)
Space Group: C 1 2 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 164.536 | α = 90 |
| b = 52.295 | β = 132.48 |
| c = 110.944 | γ = 90 |
| Software Name | Purpose |
|---|---|
| DENZO | data reduction |
| SCALEPACK | data scaling |
| SHELX | phasing |
| RESOLVE | phasing |
| REFMAC | refinement |
| PDB_EXTRACT | data extraction |
| ADSC | data collection |
Entry History
Deposition Data
- Released Date: 2007-07-31 Deposition Author(s): Rabeh, W.M., Nedyalkova, L., Tempel, W., Landry, R., Crombet, L., Kozieradzki, I., Senisterra, G., Vedadi, M., Arrowsmith, C.H., Edwards, A.M., Sundstrom, M., Weigelt, J., Bochkarev, A., Park, H., Structural Genomics Consortium (SGC)
Revision History (Full details and data files)
- Version 1.0: 2007-07-31
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Refinement description, Version format compliance - Version 1.2: 2017-10-25
Changes: Refinement description - Version 1.3: 2024-10-30
Changes: Data collection, Database references, Derived calculations, Structure summary
