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Mertk kinase domain in complex with a bisaminopyrimidine inhibitor

Analyse Mertk kinase domain in complex with a bisaminopyrimidine inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7AVZ
Type: protein
Length: 268 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosine-protein kinase mer
EC: 2.7.10.1
UniProt: Q12866
Ligands: S4N
Pockets: 1 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein kinase mer (EC 2.7.10.1)	protein	268	44% helix, 19% strand	Q12866

Ligands and binding sites

S4N · (R)-N2-(4-(cyclopropylmethoxy)-3,5-difluorophenyl)-5-(3-methylpiperazin-1-yl)-N4-(tetrahydro-2H-pyran-4-yl)pyrimidine-2,4-diamine · 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	301	0.63	0.80	33	S4N

Compared structures

7AVZ · MerTK kinase domain in complex with a bisaminopyrimidine inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
Q12866 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase mer (Q12866) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 Q12866
Elsewhere: RCSB PDB 7AVZ · PDBe 7AVZ · UniProt Q12866

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