Chlorine in PDB 6t7p: Human Plasmakallikrein Protease Domain in Complex with Active Site Directed Inhibitor

All present enzymatic activity of Human Plasmakallikrein Protease Domain in Complex with Active Site Directed Inhibitor:
3.4.21.34;

The structure of Human Plasmakallikrein Protease Domain in Complex with Active Site Directed Inhibitor, PDB code: 6t7p was solved by M.Renatus, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.13 / 1.42
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.100, 59.150, 86.720, 90.00, 90.00, 90.00
R / Rfree (%)	15.2 / 18.8

The binding sites of Chlorine atom in the Human Plasmakallikrein Protease Domain in Complex with Active Site Directed Inhibitor (pdb code 6t7p). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Human Plasmakallikrein Protease Domain in Complex with Active Site Directed Inhibitor, PDB code: 6t7p:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Human Plasmakallikrein Protease Domain in Complex with Active Site Directed Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Plasmakallikrein Protease Domain in Complex with Active Site Directed Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl314 b:21.1 occ:0.51 CL A:MU8314 0.0 21.1 0.5 C19 A:MU8314 1.5 14.5 0.5 C18 A:MU8314 1.7 51.5 0.5 C17 A:MU8314 2.3 31.3 0.5 C20 A:MU8314 2.6 15.7 0.5 C16 A:MU8314 2.7 31.2 0.5 C17 A:MU8314 2.7 19.7 0.5 O A:HIS40 2.9 18.2 1.0 O A:HOH531 3.1 31.5 1.0 C18 A:MU8314 3.7 19.0 0.5 CD1 A:ILE151 3.8 22.5 1.0 O A:HOH637 3.8 40.3 1.0 CA A:LEU41 3.9 15.4 0.8 CA A:LEU41 3.9 15.3 0.2 NH1 A:ARG39 3.9 54.2 1.0 C15 A:MU8314 3.9 19.9 1.0 C A:HIS40 4.0 16.2 1.0 C19 A:MU8314 4.0 40.5 0.5 O A:LEU41 4.1 16.6 1.0 CD2 A:LEU41 4.2 26.2 0.8 CG1 A:ILE151 4.2 22.9 1.0 C20 A:MU8314 4.3 28.3 0.5 C A:LEU41 4.4 13.8 1.0 N A:LEU41 4.4 15.4 1.0 C16 A:MU8314 4.5 19.8 0.5 CA A:GLY193 4.5 15.1 1.0 CD2 A:HIS40 4.6 15.9 1.0 CG A:LEU41 4.9 18.4 0.2 CB A:LEU41 4.9 17.8 0.2 CB A:LEU41 4.9 19.4 0.8 CZ A:ARG39 4.9 55.6 1.0 N A:GLY193 5.0 16.7 1.0 CL A:MU8314 5.0 32.3 0.5

Chlorine binding site 2 out of 2 in the Human Plasmakallikrein Protease Domain in Complex with Active Site Directed Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Human Plasmakallikrein Protease Domain in Complex with Active Site Directed Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl314 b:32.3 occ:0.49 CL A:MU8314 0.0 32.3 0.5 C19 A:MU8314 1.6 40.5 0.5 C18 A:MU8314 1.7 19.0 0.5 C17 A:MU8314 2.3 19.7 0.5 C17 A:MU8314 2.7 31.3 0.5 C20 A:MU8314 2.7 28.3 0.5 C16 A:MU8314 2.8 19.8 0.5 C18 A:MU8314 3.7 51.5 0.5 CZ A:PHE143 3.7 27.8 1.0 C19 A:MU8314 4.0 14.5 0.5 C15 A:MU8314 4.0 19.9 1.0 CD A:LYS192 4.2 27.3 1.0 CE2 A:PHE143 4.3 26.5 1.0 C20 A:MU8314 4.4 15.7 0.5 O A:HOH615 4.5 50.6 1.0 C16 A:MU8314 4.5 31.2 0.5 CE1 A:PHE143 4.5 23.5 1.0 O A:HOH637 4.6 40.3 1.0 CB A:LYS192 4.7 19.7 1.0 NZ A:LYS192 5.0 37.6 1.0 CG A:LYS192 5.0 24.3 1.0 CL A:MU8314 5.0 21.1 0.5

E.Lorthiois, J.Roache, D.Barnes-Seeman, E.Altmann, U.Hassiepen, G.Turner, R.Duvadie, V.Hornak, R.G.Karki, N.Schiering, W.A.Weihofen, F.Perruccio, A.Calhoun, T.Fazal, D.Dedic, C.Durand, S.Dussauge, K.Fettis, F.Tritsch, C.Dentel, A.Druet, D.Liu, L.Kirman, J.Lachal, K.Namoto, D.Bevan, R.Mo, G.Monnet, L.Muller, R.Zessis, X.Huang, L.Lindsley, T.Currie, Y.H.Chiu, C.Fridrich, P.Delgado, S.Wang, M.Hollis-Symynkywicz, J.Berghausen, E.Williams, H.Liu, G.Liang, H.Kim, P.Hoffmann, A.Hein, P.Ramage, A.D'arcy, S.Harlfinger, M.Renatus, S.Ruedisser, D.Feldman, J.Elliott, R.Sedrani, J.Maibaum, C.M.Adams. Structure-Based Design and Preclinical Characterization of Selective and Orally Bioavailable Factor Xia Inhibitors: Demonstrating the Power of An Integrated S1 Protease Family Approach. J.Med.Chem. V. 63 8088 2020.
ISSN: ISSN 0022-2623
PubMed: 32551603
DOI: 10.1021/ACS.JMEDCHEM.0C00279