MolNFT v1 · #115905 · protein

Syk catalytic domain complexed with a potent orally bioavailable thiazole inhibitor

5CXH · Tyrosine-protein kinase syk: “Syk catalytic domain complexed with a potent orally bioavailable thiazole inhibitor”. X-ray diffraction, 1 ligand (55M), 3 pockets (best druggability 0.62). MolNFT v1 #115905 on GenesisL1: 3D structure…

PDB: 5CXH
Type: protein
Length: 277 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: 55M
Pockets: 3 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein kinase syk (EC 2.7.10.2)	protein	277	40% helix, 22% strand	P43405

Ligands and binding sites

55M · (4R)-4-[(1R)-1-{[6-(3,4-dimethoxyphenyl)[1,3]thiazolo[5,4-c]pyridin-4-yl]oxy}ethyl]pyrrolidin-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	194	0.62	0.83	28	55M
2	57	0.29	0.75	15	empty
3	52	0.26	0.74	20	empty

Compared structures

5CXH · SYK catalytic domain complexed with a potent orally bioavailable thiazole 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 5CXH · PDBe 5CXH · UniProt P43405

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