MolNFT v1 · #115926 · protein

Syk catalytic domain complexed with a potent and orally bioavailable benzisothiazole inhibitor

5CY3 · Tyrosine-protein kinase syk: “Syk catalytic domain complexed with a potent and orally bioavailable benzisothiazole inhibitor”. X-ray diffraction, 1 ligand (55Y), 3 pockets (best druggability 0.64). MolNFT v1 #115926 on GenesisL1: 3D…

PDB: 5CY3
Type: protein
Length: 276 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: 55Y
Pockets: 3 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein kinase syk (EC 2.7.10.2)	protein	276	40% helix, 23% strand	P43405

Ligands and binding sites

55Y · (5R)-5-[(1R)-1-{[6-(1-methyl-1H-pyrazol-4-yl)-2,1-benzothiazol-4-yl]oxy}ethyl]-1,3-oxazolidin-2-one · ligand · chains A

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

Pockets

3 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	178	0.64	0.85	31	55Y
2	66	0.32	0.75	14	empty
3	51	0.27	0.74	16	empty

Compared structures

5CY3 · SYK catalytic domain complexed with a potent and orally bioavailable benzisothiazole… · 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 5CY3 · PDBe 5CY3 · UniProt P43405

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