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The kinase domain of human spleen tyrosine (syk) in complex with GTC000226

Analyse The kinase domain of human spleen tyrosine (syk) in complex with GTC000226 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4YJS
Type: protein
Length: 257 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: 4DN
Pockets: 2 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein kinase syk (EC 2.7.10.2)	protein	257	41% helix, 22% strand	P43405

Ligands and binding sites

4DN · 3-[{2-[(1,1-dioxido-2,3-dihydro-1,2-benzothiazol-6-yl)amino]pyrimidin-4-yl}(1H-indazol-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	267	0.61	0.79	33	4DN
2	57	0.30	0.76	14	empty

Compared structures

4YJS · The kinase domain of human spleen tyrosine (syk) in complex with GTC000226 · 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 4YJS · PDBe 4YJS · UniProt P43405

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