Chlorine in PDB 3p7c: P38 Inhibitor-Bound

All present enzymatic activity of P38 Inhibitor-Bound:
2.7.11.24;

The structure of P38 Inhibitor-Bound, PDB code: 3p7c was solved by K.K.Moffett, H.Namboodiri, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.09 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	66.860, 70.770, 76.130, 90.00, 90.00, 90.00
R / Rfree (%)	23.4 / 29.2

The binding sites of Chlorine atom in the P38 Inhibitor-Bound (pdb code 3p7c). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the P38 Inhibitor-Bound, PDB code: 3p7c:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the P38 Inhibitor-Bound


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of P38 Inhibitor-Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl362 b:21.8 occ:1.00 CL1 A:P7C362 0.0 21.8 1.0 C24 A:P7C362 1.7 19.4 1.0 C20 A:P7C362 2.7 20.1 1.0 C16 A:P7C362 2.7 17.5 1.0 N15 A:P7C362 3.0 17.2 1.0 CL2 A:P7C362 3.1 27.6 1.0 CD1 A:LEU75 3.3 25.1 1.0 CD1 A:LEU104 3.4 22.0 1.0 CB A:LEU104 3.6 21.3 1.0 CD A:LYS53 3.9 23.6 1.0 OE1 A:GLU71 3.9 22.5 1.0 C17 A:P7C362 4.0 17.7 1.0 CB A:LYS53 4.0 23.5 1.0 C19 A:P7C362 4.0 21.7 1.0 C13 A:P7C362 4.1 17.9 1.0 CG A:LEU104 4.2 20.0 1.0 CD1 A:ILE84 4.2 20.4 1.0 C23 A:P7C362 4.5 19.8 1.0 CG A:LYS53 4.5 24.8 1.0 CD A:GLU71 4.7 23.5 1.0 CG A:LEU75 4.7 23.1 1.0 O A:LEU104 4.7 22.3 1.0 C A:LEU104 4.8 20.9 1.0 CA A:LEU104 4.8 21.1 1.0 N12 A:P7C362 4.9 18.5 1.0 O14 A:P7C362 4.9 19.2 1.0

Chlorine binding site 2 out of 2 in the P38 Inhibitor-Bound


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of P38 Inhibitor-Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl362 b:27.6 occ:1.00 CL2 A:P7C362 0.0 27.6 1.0 C20 A:P7C362 1.7 20.1 1.0 C19 A:P7C362 2.7 21.7 1.0 C24 A:P7C362 2.8 19.4 1.0 CL1 A:P7C362 3.1 21.8 1.0 O A:ALA51 3.4 25.6 1.0 O A:LEU104 3.5 22.3 1.0 N A:LYS53 3.5 25.2 1.0 CB A:LYS53 3.5 23.5 1.0 CG2 A:THR106 3.6 16.8 1.0 C A:ALA51 3.9 24.9 1.0 C23 A:P7C362 4.0 19.8 1.0 C16 A:P7C362 4.1 17.5 1.0 N A:THR106 4.1 20.8 1.0 C A:VAL52 4.1 24.8 1.0 CA A:LYS53 4.1 24.5 1.0 C A:LEU104 4.2 20.9 1.0 CB A:THR106 4.2 20.9 1.0 N A:VAL52 4.3 24.6 1.0 CB A:ALA51 4.3 23.3 1.0 CA A:VAL52 4.3 23.9 1.0 C17 A:P7C362 4.5 17.7 1.0 CA A:VAL105 4.5 20.9 1.0 C A:VAL105 4.5 20.5 1.0 N A:VAL105 4.6 21.0 1.0 CB A:LEU104 4.6 21.3 1.0 CA A:ALA51 4.7 23.6 1.0 CD1 A:ILE84 4.8 20.4 1.0 CA A:THR106 4.8 20.4 1.0 CG A:LYS53 4.9 24.8 1.0 O A:VAL52 4.9 25.4 1.0

K.Moffett, Z.Konteatis, D.Nguyen, R.Shetty, J.Ludington, T.Fujimoto, K.J.Lee, X.Chai, H.Namboodiri, M.Karpusas, B.Dorsey, F.Guarnieri, M.Bukhtiyarova, E.Springman, E.Michelotti. Discovery of A Novel Class of Non-Atp Site Dfg-Out State P38 Inhibitors Utilizing Computationally Assisted Virtual Fragment-Based Drug Design (Vfbdd). Bioorg.Med.Chem.Lett. V. 21 7155 2011.
ISSN: ISSN 0960-894X
PubMed: 22014550
DOI: 10.1016/J.BMCL.2011.09.078