Research workbench
Human EphA3 Kinase domain in complex with ligand 90
Analyse Human EphA3 Kinase domain in complex with ligand 90 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GK4
- Type
- protein
- Length
- 275 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.1
- Source
- Homo sapiens
- Molecule
- EPH receptor A3
- EC
- 2.7.10.1
- UniProt
- Q6P4R6
- Ligands
- L90
- Pockets
- 1 · best druggability 0.61
Structure
x-ray diffraction · resolution 2.1 · 1 distinct chain · 39% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | EPH receptor A3 (EC 2.7.10.1) | protein | 275 | 39% helix, 19% strand | Q6P4R6 |
Ligands and binding sites
- L90 · 8-butyl-1-methyl-7-(5-methyl-1H-indazol-4-yl)-1H-imidazo[2,1-f]purine-2,4(3H,8H)-dione · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 312 | 0.61 | 0.78 | 31 | L90 |
Compared structures
- 4GK4 · Human EPHA3 kinase domain in complex with ligand 90 · the same entry in another collection · chain A against A, TM-score 1.00
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 Q6P4R6
- Elsewhere: RCSB PDB 4GK4 · PDBe 4GK4 · UniProt Q6P4R6
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