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Structure of L1196M mutant anaplastic lymphoma kinase in complex with crizotinib

Analyse Structure of L1196M mutant anaplastic lymphoma kinase in complex with crizotinib in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2YFX
Type: protein
Length: 292 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosine-protein kinase receptor
EC: 2.7.10.1
UniProt: B6EXY4
Ligands: VGH
Pockets: 1 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein kinase receptor (EC 2.7.10.1)	protein	292	43% helix, 14% strand	B6EXY4

Ligands and binding sites

VGH · 3-[(1R)-1-(2,6-dichloro-3-fluorophenyl)ethoxy]-5-(1-piperidin-4-yl-1H-pyrazol-4-yl)pyridin-2-amine · 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	373	0.62	0.77	43	VGH

Compared structures

2YFX · Structure of L1196M Mutant Anaplastic Lymphoma Kinase in Complex with Crizotinib · 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 B6EXY4
Elsewhere: RCSB PDB 2YFX · PDBe 2YFX · UniProt B6EXY4

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