Chlorine in PDB 5bqg: Crystal Structure of Mpges-1 Bound to An Inhibitor

All present enzymatic activity of Crystal Structure of Mpges-1 Bound to An Inhibitor:
5.3.99.3;

The structure of Crystal Structure of Mpges-1 Bound to An Inhibitor, PDB code: 5bqg was solved by M.J.Fisher, M.A.Schiffler, S.L.Kuklish, S.Antonysamy, J.G.Luz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.98 / 1.44
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	77.472, 77.472, 123.123, 90.00, 90.00, 120.00
R / Rfree (%)	15 / 16.9

The binding sites of Chlorine atom in the Crystal Structure of Mpges-1 Bound to An Inhibitor (pdb code 5bqg). 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 Mpges-1 Bound to An Inhibitor, PDB code: 5bqg:

Chlorine binding site 1 out of 1 in the Crystal Structure of Mpges-1 Bound to 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 Mpges-1 Bound to An Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:19.9 occ:0.65 CL A:4UJ201 0.0 19.9 0.7 C5 A:4UJ201 1.7 20.3 1.0 C6 A:4UJ201 2.7 22.4 1.0 C4 A:4UJ201 2.7 24.6 1.0 C3 A:4UJ201 3.1 29.1 1.0 O A:4UJ201 3.1 33.0 1.0 OG A:SER127 3.4 15.6 1.0 O A:HOH367 3.8 17.3 1.0 C7 A:4UJ201 4.0 19.9 1.0 C9 A:4UJ201 4.0 22.8 1.0 N1 A:4UJ201 4.1 22.8 1.0 CB A:ALA123 4.2 16.5 1.0 NH2 A:ARG126 4.3 12.2 1.0 C8 A:4UJ201 4.5 24.9 1.0 CB A:SER127 4.6 14.1 1.0 SG2 A:GSH202 4.8 12.0 1.0

M.A.Schiffler, S.Antonysamy, S.N.Bhattachar, K.M.Campanale, S.Chandrasekhar, B.Condon, P.V.Desai, M.J.Fisher, C.Groshong, A.Harvey, M.J.Hickey, N.E.Hughes, S.A.Jones, E.J.Kim, S.L.Kuklish, J.G.Luz, B.H.Norman, R.E.Rathmell, J.R.Rizzo, T.W.Seng, S.J.Thibodeaux, T.A.Woods, J.S.York, X.P.Yu. Discovery and Characterization of 2-Acylaminoimidazole Microsomal Prostaglandin E Synthase-1 Inhibitors. J.Med.Chem. V. 59 194 2016.
ISSN: ISSN 0022-2623
PubMed: 26653180
DOI: 10.1021/ACS.JMEDCHEM.5B01249