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Syk catalytic domain complexed with a potent triazine inhibitor

Analyse Syk catalytic domain complexed with a potent triazine inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4RX7
Type: protein
Length: 272 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: 3YV
Pockets: 1 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein kinase syk (EC 2.7.10.2)	protein	272	42% helix, 22% strand	P43405

Ligands and binding sites

3YV · 3-{[(1R,2S)-2-aminocyclohexyl]amino}-5-{[3-(2H-1,2,3-triazol-2-yl)phenyl]amino}-1,2,4-triazine-6-carboxamide · ligand · chains A
FMT · Formic acid · additive · chains A
GOL · Glycerol · additive · 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	315	0.62	0.79	35	GOL, 3YV

Compared structures

4RX7 · SYK Catalytic Domain Complexed with a Potent Triazine 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 4RX7 · PDBe 4RX7 · UniProt P43405

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