Download MendeleyTemperature Gradient Structures of Oncogenic KRAS G12C Mutants
Deck, S.L., Xu, M., Aplin, C., Milano, S.K.To be published.
8TXJ | pdb_00008txj
KRAS 1-169 G12C Mutant at 277k
- PDB DOI: https://doi.org/10.2210/pdb8TXJ/pdb
- Classification: HYDROLASE
- Organism(s): Homo sapiens
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): Yes
- Deposited: 2023-08-23 Released: 2024-08-28
- Funding Organization(s): National Institutes of Health/National Cancer Institute (NIH/NCI), National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.40 Å
- R-Value Free: 0.206 (Depositor), 0.210 (DCC)
- R-Value Work: 0.187 (Depositor), 0.190 (DCC)
- R-Value Observed: 0.188 (Depositor)
Starting Model: experimental
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This is version 1.0 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 |
| Isoform 2B of GTPase KRas | 169 | Homo sapiens | Mutation(s): 1 Gene Names: KRAS, KRAS2, RASK2 EC: 3.6.5.2 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P01116 (Homo sapiens) Explore P01116 Go to UniProtKB: P01116 | |||||
PHAROS: P01116 GTEx: ENSG00000133703 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P01116 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| GDP (Subject of Investigation/LOI) Query on GDP | B [auth A] | GUANOSINE-5'-DIPHOSPHATE C10 H15 N5 O11 P2 QGWNDRXFNXRZMB-UUOKFMHZSA-N |  | ||
| MG (Subject of Investigation/LOI) Query on MG | C [auth A] | MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.40 Å
- R-Value Free: 0.206 (Depositor), 0.210 (DCC)
- R-Value Work: 0.187 (Depositor), 0.190 (DCC)
- R-Value Observed: 0.188 (Depositor)
Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 39.418 | α = 90 |
| b = 41.207 | β = 90 |
| c = 92.101 | γ = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| autoPROC | data reduction |
| autoPROC | data scaling |
| PHASER | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2024-08-28 Deposition Author(s): Deck, S.L., Xu, M., Milano, S.K., Aplin, C.
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Institutes of Health/National Cancer Institute (NIH/NCI) | United States | CA201402 |
| National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | United States | P30GM124166 |
Revision History (Full details and data files)
- Version 1.0: 2024-08-28
Type: Initial release
