Chlorine in PDB 2jlq: Dengue Virus 4 NS3 Helicase Structure, Apo Enzyme.

All present enzymatic activity of Dengue Virus 4 NS3 Helicase Structure, Apo Enzyme.:
3.4.21.91;

The structure of Dengue Virus 4 NS3 Helicase Structure, Apo Enzyme., PDB code: 2jlq was solved by D.H.Luo, T.Xu, R.P.Watson, D.S.Becker, A.Sampath, W.Jahnke, S.S.Yeong, C.H.Wang, S.P.Lim, S.G.Vasudevan, J.Lescar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.96 / 1.67
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	52.821, 92.614, 102.962, 90.00, 90.00, 90.00
R / Rfree (%)	21.095 / 23.384

The binding sites of Chlorine atom in the Dengue Virus 4 NS3 Helicase Structure, Apo Enzyme. (pdb code 2jlq). 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 Dengue Virus 4 NS3 Helicase Structure, Apo Enzyme., PDB code: 2jlq:

Chlorine binding site 1 out of 1 in the Dengue Virus 4 NS3 Helicase Structure, Apo Enzyme.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Dengue Virus 4 NS3 Helicase Structure, Apo Enzyme. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1619 b:37.4 occ:1.00 OG1 A:THR408 2.9 24.9 1.0 N A:ARG387 3.0 29.7 1.0 NH2 A:ARG387 3.3 38.2 1.0 CB A:ARG387 3.6 31.0 1.0 CB A:THR408 3.7 24.1 1.0 CG A:ARG387 3.8 32.9 1.0 CB A:SER386 3.8 28.2 1.0 CA A:ARG387 3.9 31.0 1.0 CA A:SER386 3.9 27.9 1.0 CG2 A:THR408 3.9 24.6 1.0 C A:SER386 3.9 28.6 1.0 CD A:ARG387 4.0 35.9 1.0 O A:HOH2186 4.1 32.9 1.0 CZ A:ARG387 4.4 39.0 1.0 OD2 A:ASP409 4.6 28.5 1.0 NE A:ARG387 4.7 37.2 1.0 CB A:ILE410 4.7 25.8 1.0 OG A:SER386 4.8 28.5 1.0 CG2 A:ILE410 4.9 25.0 1.0

D.Luo, T.Xu, R.P.Watson, D.Scherer-Becker, A.Sampath, W.Jahnke, S.S.Yeong, C.H.Wang, S.P.Lim, A.Strongin, S.G.Vasudevan, J.Lescar. Insights Into Rna Unwinding and Atp Hydrolysis By the Flavivirus NS3 Protein. Embo J. V. 27 3209 2008.
ISSN: ISSN 0261-4189
PubMed: 19008861
DOI: 10.1038/EMBOJ.2008.232