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Human EPHA3 kinase domain in complex with quinoxaline derivatives

Analyse Human EPHA3 kinase domain in complex with quinoxaline derivatives in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4P5Q
Type: protein
Length: 275 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ephrin type-a receptor 3
EC: 2.7.10.1
UniProt: P29320
Ligands: Q0B
Pockets: 1 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ephrin type-a receptor 3 (EC 2.7.10.1)	protein	275	40% helix, 18% strand	P29320

Ligands and binding sites

Q0B · 2-amino-1-(2-chlorophenyl)-N-(3-ethoxypropyl)-1H-pyrrolo[2,3-b]quinoxaline-3-carboxamide · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	280	0.58	0.78	33	Q0B

Compared structures

4P5Q · Human EphA3 Kinase domain in complex with quinoxaline derivatives · the same entry in another collection · chain A against A, TM-score 1.00
P29320 · AlphaFold monomer V2.0 prediction for ephrin type-a receptor 3 (P29320) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P29320
Elsewhere: RCSB PDB 4P5Q · PDBe 4P5Q · UniProt P29320

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