Chlorine in PDB 5cxz: Syk Catalytic Domain Complexed with Naphthyridine Inhibitor

All present enzymatic activity of Syk Catalytic Domain Complexed with Naphthyridine Inhibitor:
2.7.10.2;

The structure of Syk Catalytic Domain Complexed with Naphthyridine Inhibitor, PDB code: 5cxz was solved by G.Thoma, S.Veenstra, R.Strang, J.Blanz, E.Vangrevelinghe, J.Berghausen, C.C.Lee, H.-G.Zerwes, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.22 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	40.080, 87.980, 88.500, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 20.8

The binding sites of Chlorine atom in the Syk Catalytic Domain Complexed with Naphthyridine Inhibitor (pdb code 5cxz). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Syk Catalytic Domain Complexed with Naphthyridine Inhibitor, PDB code: 5cxz:

Chlorine binding site 1 out of 1 in the Syk Catalytic Domain Complexed with Naphthyridine Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Syk Catalytic Domain Complexed with Naphthyridine Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl702 b:29.9 occ:1.00 N A:LYS537 3.2 12.7 1.0 N A:VAL536 3.4 20.0 1.0 CB A:LYS537 3.7 11.7 1.0 C A:PRO535 3.7 21.9 1.0 CG2 A:VAL536 3.7 26.7 1.0 CG A:LYS537 3.7 8.9 1.0 CZ3 A:TRP538 3.8 10.1 1.0 CA A:PRO535 3.9 22.0 1.0 CD A:LYS537 4.0 14.8 1.0 CA A:LYS537 4.1 10.8 1.0 CE3 A:TRP538 4.1 8.9 1.0 CA A:VAL536 4.1 19.3 1.0 C A:VAL536 4.1 19.1 1.0 O A:PRO535 4.4 18.5 1.0 O A:TRP534 4.4 30.1 1.0 CB A:VAL536 4.5 25.8 1.0 CB A:PRO535 4.8 22.9 1.0 CE A:LYS537 4.9 19.9 1.0

G.Thoma, S.Veenstra, R.Strang, J.Blanz, E.Vangrevelinghe, J.Berghausen, C.C.Lee, H.G.Zerwes. Orally Bioavailable Syk Inhibitors with Activity in A Rat Pk/Pd Model. Bioorg.Med.Chem.Lett. V. 25 4642 2015.
ISSN: ESSN 1464-3405
PubMed: 26320624
DOI: 10.1016/J.BMCL.2015.08.037