MolNFT v1 · #106374 · protein

Syk catalytic domain complexed with a potent triazine INHIBITOR2

4RX8 · Tyrosine-protein kinase syk: “Syk catalytic domain complexed with a potent triazine INHIBITOR2”. X-ray diffraction, 1 ligand (3YX), 2 pockets (best druggability 0.62). MolNFT v1 #106374 on GenesisL1: 3D structure, binding sites and…

PDB: 4RX8
Type: protein
Length: 269 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: 3YX
Pockets: 2 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein kinase syk (EC 2.7.10.2)	protein	269	42% helix, 23% strand	P43405

Ligands and binding sites

3YX · 3-{[(1R,2S)-2-aminocyclohexyl]amino}-5-(1H-indol-7-ylamino)-1,2,4-triazine-6-carboxamide · ligand · chains A
GOL · Glycerol · additive · 2 copies · 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	319	0.62	0.79	32	GOL, 3YX
2	57	0.30	0.75	15	empty

Compared structures

4RX8 · SYK Catalytic Domain Complexed with a Potent Triazine Inhibitor2 · 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 4RX8 · PDBe 4RX8 · UniProt P43405

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