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Crystal structure of TYK2 kinase with compound 14

Analyse Crystal structure of TYK2 kinase with compound 14 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6VNV
Type: protein
Length: 275 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Non-receptor tyrosine-protein kinase TYK2
EC: 2.7.10.2
UniProt: P29597
Ligands: R4Y
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Non-receptor tyrosine-protein kinase TYK2 (EC 2.7.10.2)	protein	275	43% helix, 20% strand	P29597

Ligands and binding sites

R4Y · (1S,2S)-2-cyano-N-[(1S,5R)-3-(5-fluoro-2-{[1-(2-hydroxyethyl)-1H-pyrazol-4-yl]amino}pyrimidin-4-yl)-3-azabicyclo[3.1.0]hexan-1-yl]cyclopropane-1-carboxamide · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	523	0.72	0.81	53	R4Y
2	55	0.28	0.74	15	empty

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

6VNV · Crystal structure of TYK2 kinase with compound 14 · 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 P29597
Elsewhere: RCSB PDB 6VNV · PDBe 6VNV · UniProt P29597

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