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Crystal structures of spleen tyrosine kinase in complex with a novel inhibitor

Analyse Crystal structures of spleen tyrosine kinase in complex with a novel inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5Y5T
Type: protein
Length: 263 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosine-protein kinase syk
EC: 2.7.10.2
UniProt: P43405
Ligands: 8OR
Pockets: 2 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein kinase syk (EC 2.7.10.2)	protein	263	40% helix, 19% strand	P43405

Ligands and binding sites

8OR · 2-[[(1S,2S)-2-azanylcyclohexyl]amino]-4-[(4-methylsulfonylphenyl)amino]-6H-pyrido[4,3-d]pyrimidin-5-one · 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	293	0.57	0.77	39	8OR
2	71	0.33	0.75	19	empty

Compared structures

5Y5T · Crystal structures of spleen tyrosine kinase in complex with a novel inhibitor · 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 P43405
Elsewhere: RCSB PDB 5Y5T · PDBe 5Y5T · UniProt P43405

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