MolNFT v1 · #115922 · protein

Syk catalytic domain complexed with naphthyridine inhibitor

5CXZ · Tyrosine-protein kinase syk: “Syk catalytic domain complexed with naphthyridine inhibitor”. X-ray diffraction, 2 ligands (55U, CL), 1 pocket (best druggability 0.63). MolNFT v1 #115922 on GenesisL1: 3D structure, binding sites and…

PDB: 5CXZ
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: 55U, CL
Pockets: 1 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein kinase syk (EC 2.7.10.2)	protein	269	40% helix, 23% strand	P43405

Ligands and binding sites

55U · N-{7-[4-(dimethylamino)phenyl]-1,6-naphthyridin-5-yl}propane-1,3-diamine · ligand · chains A
CL · Chloride ion · ion · 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	348	0.63	0.78	43	55U

Compared structures

5CXZ · SYK catalytic domain complexed with naphthyridine 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 5CXZ · PDBe 5CXZ · UniProt P43405

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