MolNFT v1 · #111195 · protein

Syk kinase domain in complex with inhibitor GTC000224

4YJQ · Tyrosine-protein kinase syk: “Syk kinase domain in complex with inhibitor GTC000224”. X-ray diffraction, 1 ligand (4DK), 2 pockets (best druggability 0.62). MolNFT v1 #111195 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 4YJQ
Type: protein
Length: 266 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: 4DK
Pockets: 2 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein kinase syk (EC 2.7.10.2)	protein	266	38% helix, 23% strand	P43405

Ligands and binding sites

4DK · 3-[1H-indazol-4-yl(2-{[3-(4-methyl-1,3-oxazol-5-yl)phenyl]amino}pyrimidin-4-yl)amino]propan-1-ol · 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	269	0.62	0.80	30	4DK
2	54	0.30	0.76	17	empty

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

4YJQ · SYK kinase domain in complex with inhibitor GTC000224 · 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 4YJQ · PDBe 4YJQ · UniProt P43405

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