Download MendeleyCrystal structure of human Ras-related GTP-binding D.
Mulichak, A.M., Rabeh, W.M., Tempel, W., Nedyalkova, L., Landry, R., Arrowsmith, C.H., Edwards, A.M., Sundstrom, M., Weigelt, J., Keefe, L.J., Bochkarev, A., Park, H.To be published.
2Q3F
X-ray crystal structure of putative human Ras-related GTP binding D in complex with GMPPNP
- PDB DOI: https://doi.org/10.2210/pdb2Q3F/pdb
- Classification: PROTEIN BINDING
- Organism(s): Homo sapiens
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): Yes
- Deposited: 2007-05-30 Released: 2007-06-12
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.10 Å
- R-Value Free: 0.268
- R-Value Work: 0.221
- R-Value Observed: 0.223
This is version 1.2 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 |
| Ras-related GTP-binding protein D | 181 | Homo sapiens | Mutation(s): 4 Gene Names: RRAGD |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q9NQL2 (Homo sapiens) Explore Q9NQL2 Go to UniProtKB: Q9NQL2 | |||||
PHAROS: Q9NQL2 GTEx: ENSG00000025039 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9NQL2 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| GNP Query on GNP | D [auth A], F [auth B] | PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER C10 H17 N6 O13 P3 UQABYHGXWYXDTK-UUOKFMHZSA-N |  | ||
| MG Query on MG | C [auth A], E [auth B] | MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N |  | ||
| 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: 2.10 Å
- R-Value Free: 0.268
- R-Value Work: 0.221
- R-Value Observed: 0.223
- Space Group: P 1 21 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 47.73 | α = 90 |
| b = 67.13 | β = 110.92 |
| c = 66.36 | γ = 90 |
| Software Name | Purpose |
|---|---|
| JDirector | data collection |
| SOLVE | phasing |
| CNS | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
Entry History
Deposition Data
- Released Date: 2007-06-12 Deposition Author(s): Mulichak, A.M., Rabeh, W.M., Tempel, W., Nedyalkova, L., Landry, R., Arrowsmith, C.H., Edwards, A.M., Sundstrom, M., Weigelt, J., Keefe, L.J., Bochkarev, A., Park, H., Structural Genomics Consortium (SGC)
Revision History (Full details and data files)
- Version 1.0: 2007-06-12
Type: Initial release - Version 1.1: 2008-05-01
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Version format compliance
