Download MendeleyHigh resolution crystal structures of the death associated protein kinase catalytic domain with a key point mutation in the glycine-rich loop
McNamara, L.K., Schavocky, J.P., Watterson, D.M., Brunzelle, J.S.To be published.
3DFC
Crystal structure of a glycine-rich loop mutant of the death associated protein kinase catalytic domain with AMPPNP
- PDB DOI: https://doi.org/10.2210/pdb3DFC/pdb
- Classification: TRANSFERASE
- Organism(s): Homo sapiens
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2008-06-11 Released: 2009-05-26
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.90 ?
- R-Value Free: 0.230
- R-Value Work: 0.165
- R-Value Observed: 0.168
Starting Model: experimental
View more details
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 |
| Death-associated protein kinase 1 | A [auth B] | 295 | Homo sapiens | Mutation(s): 1 Gene Names: DAPK1, DAPK EC: 2.7.11.1 |  |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P53355 (Homo sapiens) Explore P53355 Go to UniProtKB: P53355 | |||||
PHAROS: P53355 GTEx: ENSG00000196730 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P53355 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| ANP Query on ANP | B | PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER C10 H17 N6 O12 P3 PVKSNHVPLWYQGJ-KQYNXXCUSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.90 ?
- R-Value Free: 0.230
- R-Value Work: 0.165
- R-Value Observed: 0.168
- Space Group: P 21 21 21
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 46.688 | ¦Á = 90 |
| b = 62.444 | ¦Â = 90 |
| c = 88.602 | ¦Ă = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| BLU-MAX | data collection |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| PHASER | phasing |
Entry History
Deposition Data
- Released Date: 2009-05-26 Deposition Author(s): McNamara, L.K., Schavocky, J.P., Watterson, D.M., Brunzelle, J.S.
Revision History (Full details and data files)
- Version 1.0: 2009-05-26
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2016-01-27
Changes: Structure summary - Version 1.3: 2023-08-30
Changes: Data collection, Database references, Derived calculations, Refinement description
