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Mertk kinase domain with type 1 inhibitor from a DNA-encoded library

Analyse Mertk kinase domain with type 1 inhibitor from a DNA-encoded library in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7AW3
Type: protein
Length: 269 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: S4Z
Pockets: 1 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein kinase mer (EC 2.7.10.1)	protein	269	44% helix, 18% strand	Q12866

Ligands and binding sites

S4Z · 2-(1-((5-chloro-1H-pyrrolo[2,3-b]pyridine-3-carboxamido)methyl)-2-azabicyclo[2.1.1]hexan-2-yl)-N-methyl-4-(trifluoromethyl)thiazole-5-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	281	0.62	0.79	28	S4Z

Compared structures

7AW3 · MerTK kinase domain with type 1 inhibitor from a DNA-encoded library · 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 Q12866
Elsewhere: RCSB PDB 7AW3 · PDBe 7AW3 · UniProt Q12866

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