Chlorine in PDB 5mah: Crystal Structure of Melk in Complex with An Inhibitor

All present enzymatic activity of Crystal Structure of Melk in Complex with An Inhibitor:
2.7.10.2; 2.7.11.1;

The structure of Crystal Structure of Melk in Complex with An Inhibitor, PDB code: 5mah was solved by G.Canevari, S.Re Depaolini, E.Casale, E.Felder, B.Kuster, S.Heinzlmeir, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.55 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.667, 63.704, 90.945, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 23.7

The structure of Crystal Structure of Melk in Complex with An Inhibitor also contains other interesting chemical elements:

Fluorine	(F)	3 atoms
Sodium	(Na)	2 atoms

The binding sites of Chlorine atom in the Crystal Structure of Melk in Complex with An Inhibitor (pdb code 5mah). 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 Crystal Structure of Melk in Complex with An Inhibitor, PDB code: 5mah:

Chlorine binding site 1 out of 1 in the Crystal Structure of Melk in Complex with An Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Melk in Complex with An Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl403 b:43.4 occ:1.00 NH1 A:ARG114 3.0 28.9 1.0 N A:GLU272 3.2 28.6 1.0 NE A:ARG114 3.5 27.3 1.0 CZ A:ARG114 3.7 28.1 1.0 CA A:VAL271 3.8 29.9 1.0 CB A:GLU272 4.0 32.2 1.0 C A:VAL271 4.0 28.3 1.0 CA A:GLU272 4.1 31.9 1.0 CG A:GLU272 4.2 37.1 1.0 CE2 A:TYR269 4.3 31.8 1.0 CG1 A:VAL271 4.3 28.2 1.0 CB A:ARG114 4.3 24.7 1.0 CB A:VAL271 4.5 29.2 1.0 O A:GLU272 4.6 30.7 1.0 O A:PRO270 4.6 29.6 1.0 O A:HOH525 4.6 49.2 1.0 CD A:ARG114 4.7 26.0 1.0 OH A:TYR269 4.7 34.6 1.0 O A:HOH539 4.8 35.9 1.0 C A:GLU272 4.8 29.0 1.0 CG2 A:VAL271 4.8 28.7 1.0 O A:ARG114 4.8 22.2 1.0 N A:VAL271 4.9 29.8 1.0 CZ A:TYR269 4.9 33.0 1.0 OE1 A:GLU272 4.9 41.4 1.0 NH2 A:ARG114 5.0 27.3 1.0 CE2 A:TYR267 5.0 33.9 1.0 CG A:ARG114 5.0 25.3 1.0

S.Klaeger, S.Heinzlmeir, M.Wilhelm, H.Polzer, B.Vick, P.A.Koenig, M.Reinecke, B.Ruprecht, S.Petzoldt, C.Meng, J.Zecha, K.Reiter, H.Qiao, D.Helm, H.Koch, M.Schoof, G.Canevari, E.Casale, S.R.Depaolini, A.Feuchtinger, Z.Wu, T.Schmidt, L.Rueckert, W.Becker, J.Huenges, A.K.Garz, B.O.Gohlke, D.P.Zolg, G.Kayser, T.Vooder, R.Preissner, H.Hahne, N.Tonisson, K.Kramer, K.Gotze, F.Bassermann, J.Schlegl, H.C.Ehrlich, S.Aiche, A.Walch, P.A.Greif, S.Schneider, E.R.Felder, J.Ruland, G.Medard, I.Jeremias, K.Spiekermann, B.Kuster. The Target Landscape of Clinical Kinase Drugs. Science V. 358 2017.
ISSN: ESSN 1095-9203
PubMed: 29191878
DOI: 10.1126/SCIENCE.AAN4368