Download MendeleyStructural basis of G-protein target alternation of MgcRacGAP by phospholylation
Murayama, K., Kato-Murayama, M., Hosaka, T., Kawashima, T., Kitamura, T., Yokoyama, S., Shirouzu, M.To be published.
5C2J
Complex structure of the GAP domain of MgcRacGAP and Cdc42
- PDB DOI: https://doi.org/10.2210/pdb5C2J/pdb
- Classification: HYDROLASE ACTIVATOR/SIGNALING PROTEIN
- Organism(s): Homo sapiens, Mus musculus
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2015-06-16 Released: 2016-06-22
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.50 Å
- R-Value Free: 0.263
- R-Value Work: 0.198
- R-Value Observed: 0.198
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 |
| Rac GTPase-activating protein 1 | 208 | Homo sapiens | Mutation(s): 0 Gene Names: RACGAP1, KIAA1478, MGCRACGAP |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q9H0H5 (Homo sapiens) Explore Q9H0H5 Go to UniProtKB: Q9H0H5 | |||||
PHAROS: Q9H0H5 GTEx: ENSG00000161800 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9H0H5 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Cell division control protein 42 homolog | 198 | Mus musculus | Mutation(s): 0 Gene Names: Cdc42 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P60766 (Mus musculus) Explore P60766 Go to UniProtKB: P60766 | |||||
IMPC: MGI:106211 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P60766 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| GDP Query on GDP | D [auth B] | GUANOSINE-5'-DIPHOSPHATE C10 H15 N5 O11 P2 QGWNDRXFNXRZMB-UUOKFMHZSA-N |  | ||
| AF3 Query on AF3 | E [auth B] | ALUMINUM FLUORIDE Al F3 KLZUFWVZNOTSEM-UHFFFAOYSA-K |  | ||
| MG Query on MG | C [auth B] | MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.50 Å
- R-Value Free: 0.263
- R-Value Work: 0.198
- R-Value Observed: 0.198
- Space Group: P 1 21 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 43.324 | α = 90 |
| b = 74.237 | β = 96.67 |
| c = 55.423 | γ = 90 |
| Software Name | Purpose |
|---|---|
| CNS | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| MOLREP | phasing |
Entry History
Deposition Data
- Released Date: 2016-06-22 Deposition Author(s): Murayama, K., Kato-Murayama, M., Hosaka, T., Kitamura, T., Yokoyama, S., Shirouzu, M.
Revision History (Full details and data files)
- Version 1.0: 2016-06-22
Type: Initial release - Version 1.1: 2020-02-19
Changes: Data collection, Derived calculations - Version 1.2: 2023-11-08
Changes: Data collection, Database references, Refinement description
