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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).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEPH receptor A3 (EC 2.7.10.1)protein27539% helix, 19% strandQ6P4R6

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13120.610.7831L90

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

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