Chlorine in PDB 4nau: S. Aureus Coad with Inhibitor

All present enzymatic activity of S. Aureus Coad with Inhibitor:
2.7.7.3;

The structure of S. Aureus Coad with Inhibitor, PDB code: 4nau was solved by S.D.Lahiri, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.94 / 2.33
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	77.095, 127.782, 127.123, 90.00, 90.00, 90.00
R / Rfree (%)	25.6 / 32

The binding sites of Chlorine atom in the S. Aureus Coad with Inhibitor (pdb code 4nau). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the S. Aureus Coad with Inhibitor, PDB code: 4nau:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the S. Aureus Coad with Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of S. Aureus Coad with Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:50.0 occ:1.00 CL7 A:2W3202 0.0 50.0 1.0 C25 A:2W3202 1.7 50.0 1.0 C24 A:2W3202 2.6 50.0 1.0 CL8 A:2W3202 2.7 50.0 1.0 C26 A:2W3202 2.7 50.0 1.0 CB A:PHE71 3.0 50.0 1.0 CD2 A:PHE71 3.6 50.0 1.0 CG A:PHE71 3.7 50.0 1.0 O A:PHE71 3.8 50.0 1.0 CA A:PHE71 3.9 50.0 1.0 C A:PHE71 3.9 50.0 1.0 C23 A:2W3202 4.0 50.0 1.0 C21 A:2W3202 4.0 50.0 1.0 CD1 A:LEU75 4.2 39.0 1.0 N A:PHE71 4.3 50.0 1.0 CA A:LEU75 4.4 39.8 1.0 O A:GLY73 4.4 50.0 1.0 C22 A:2W3202 4.5 50.0 1.0 N A:LEU75 4.6 42.8 1.0 CB A:LEU75 4.7 38.7 1.0 N A:SER72 4.7 50.0 1.0 C A:LEU74 4.7 48.4 1.0 CE2 A:PHE71 4.9 50.0 1.0 O A:LEU74 4.9 50.0 1.0 O A:VAL37 4.9 45.7 1.0 CD1 A:LEU38 4.9 50.0 1.0 CB A:TYR78 4.9 46.8 1.0 CB A:CYS36 4.9 43.8 1.0 O A:SER72 4.9 50.0 1.0 C A:GLY73 5.0 50.0 1.0

Chlorine binding site 2 out of 2 in the S. Aureus Coad with Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of S. Aureus Coad with Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:50.0 occ:1.00 CL8 A:2W3202 0.0 50.0 1.0 C24 A:2W3202 1.7 50.0 1.0 C25 A:2W3202 2.5 50.0 1.0 CL7 A:2W3202 2.7 50.0 1.0 C23 A:2W3202 2.8 50.0 1.0 O A:CYS36 3.7 37.0 1.0 CB A:CYS36 3.8 43.8 1.0 C26 A:2W3202 3.9 50.0 1.0 CB A:PRO9 3.9 35.7 1.0 CD1 A:LEU75 4.0 39.0 1.0 N A:LEU38 4.1 50.0 1.0 C22 A:2W3202 4.1 50.0 1.0 C A:CYS36 4.2 36.9 1.0 C A:VAL37 4.2 45.6 1.0 CA A:LEU38 4.2 50.0 1.0 O A:VAL37 4.4 45.7 1.0 CB A:LEU38 4.4 50.0 1.0 CA A:PRO9 4.4 35.9 1.0 C21 A:2W3202 4.5 50.0 1.0 N A:GLY10 4.5 37.4 1.0 N A:VAL37 4.7 45.5 1.0 CD1 A:LEU38 4.7 50.0 1.0 CA A:CYS36 4.7 39.4 1.0 O A:GLY10 4.8 36.1 1.0 CA A:VAL37 4.9 45.2 1.0 CG A:LEU75 4.9 35.8 1.0

B.L.De Jonge, G.K.Walkup, S.D.Lahiri, H.Huynh, G.Neckermann, L.Utley, T.J.Nash, J.Brock, M.San Martin, A.Kutschke, M.Johnstone, V.Laganas, L.Hajec, R.F.Gu, H.Ni, B.Chen, K.Hutchings, E.Holt, D.Mckinney, N.Gao, S.Livchak, J.Thresher. Discovery of Inhibitors of 4'-Phosphopantetheine Adenylyltransferase (Ppat) to Validate Ppat As A Target For Antibacterial Therapy. Antimicrob.Agents Chemother. V. 57 6005 2013.
ISSN: ISSN 0066-4804
PubMed: 24041904
DOI: 10.1128/AAC.01661-13