Download MendeleyKinase Domain of Human Ephrin Type-A Receptor 5 (EphA5).
Walker, J.R., Cuerrier, D., Butler-Cole, C., Weigelt, J., Arrowsmith, C.H., Edwards, A.M., Bochkarev, A., Dhe-Paganon, S.To be published.
2R2P
Kinase domain of human ephrin type-A receptor 5 (EphA5)
- PDB DOI: https://doi.org/10.2210/pdb2R2P/pdb
- Classification: TRANSFERASE
- Organism(s): Homo sapiens
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2007-08-27 Released: 2007-09-25
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.40 Å
- R-Value Free: 0.283
- R-Value Work: 0.199
- R-Value Observed: 0.203
wwPDB Validation 3D Report Full Report
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 |
| Ephrin type-A receptor 5 | 295 | Homo sapiens | Mutation(s): 0 Gene Names: EPHA5, EHK1, HEK7 EC: 2.7.10.1 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P54756 (Homo sapiens) Explore P54756 Go to UniProtKB: P54756 | |||||
PHAROS: P54756 GTEx: ENSG00000145242 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P54756 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| SO4 Query on SO4 | B [auth A], C [auth A], D [auth A], E [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| CL Query on CL | F [auth A] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.40 Å
- R-Value Free: 0.283
- R-Value Work: 0.199
- R-Value Observed: 0.203
- Space Group: P 65 2 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 80.085 | α = 90 |
| b = 80.085 | β = 90 |
| c = 169.237 | γ = 120 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| PHASER | phasing |
Entry History
Deposition Data
- Released Date: 2007-09-25 Deposition Author(s): Walker, J.R., Cuerrier, D., Butler-Cole, C., Weigelt, J., Arrowsmith, C.H., Edwards, A.M., Bochkarev, A., Dhe-Paganon, S., Structural Genomics Consortium (SGC)
Revision History (Full details and data files)
- Version 1.0: 2007-09-25
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2023-08-30
Changes: Data collection, Database references, Refinement description
