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Crystal Structure of Ephrin A2 (EphA2) Receptor Protein Kinase with the NVP-BHG712 derivative ATDL13
Analyse Crystal Structure of Ephrin A2 (EphA2) Receptor Protein Kinase with the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Q7D
- Type
- protein
- Length
- 275 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 0.978
- Source
- Homo sapiens
- Molecule
- Ephrin type-A receptor 2
- EC
- 2.7.10.1
- UniProt
- P29317
- Ligands
- HOT
- Pockets
- 2 · best druggability 0.65
Structure
x-ray diffraction · resolution 0.978 · 1 distinct chain · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ephrin type-A receptor 2 (EC 2.7.10.1) | protein | 275 | 41% helix, 17% strand | P29317 |
Ligands and binding sites
- HOT · 3-[[4-imidazol-1-yl-6-(4-oxidanylpiperidin-1-yl)-1,3,5-triazin-2-yl]amino]-4-methyl-~{N}-[3-(trifluoromethyl)phenyl]benzamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 340 | 0.65 | 0.80 | 42 | HOT |
| 2 | 55 | 0.31 | 0.76 | 19 | empty |
Compared structures
- 6Q7D · Crystal structure of ephrin A2 (EPHA2) receptor protein kinase with the nvp-BHG712… · the same entry in another collection · chain A against A, TM-score 1.00
- P29317 · AlphaFold monomer V2.0 prediction for ephrin type-a receptor 2 (P29317) · a predicted model of the same protein · chain A against A, TM-score 0.93
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P29317
- Elsewhere: RCSB PDB 6Q7D · PDBe 6Q7D · UniProt P29317
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