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The kinase domain of human spleen tyrosine (syk) in complex with GTC000250

Analyse The kinase domain of human spleen tyrosine (syk) in complex with GTC000250 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4YJV
Type: protein
Length: 265 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: 4DT
Pockets: 1 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein kinase syk (EC 2.7.10.2)	protein	265	37% helix, 20% strand	P43405

Ligands and binding sites

4DT · 3-[6-({4-[ethyl(1H-indazol-4-yl)amino]-5-fluoropyrimidin-2-yl}amino)-2,4-dihydro-1H-indazol-1-yl]propan-1-ol · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	283	0.61	0.79	38	4DT

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

4YJV · The kinase domain of human spleen tyrosine (syk) in complex with GTC000250 · 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 4YJV · PDBe 4YJV · UniProt P43405

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