Sodium in PDB 6ts4: Coagulation Factor XI Protease Domain in Complex with Active Site Inhibitor

All present enzymatic activity of Coagulation Factor XI Protease Domain in Complex with Active Site Inhibitor:
3.4.21.27;

The structure of Coagulation Factor XI Protease Domain in Complex with Active Site Inhibitor, PDB code: 6ts4 was solved by M.Renatus, N.Schiering, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.00 / 1.17
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	60.320, 60.800, 66.870, 90.00, 90.00, 90.00
R / Rfree (%)	18.7 / 20.3

The binding sites of Sodium atom in the Coagulation Factor XI Protease Domain in Complex with Active Site Inhibitor (pdb code 6ts4). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Coagulation Factor XI Protease Domain in Complex with Active Site Inhibitor, PDB code: 6ts4:

Sodium binding site 1 out of 1 in the Coagulation Factor XI Protease Domain in Complex with Active Site Inhibitor


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Coagulation Factor XI Protease Domain in Complex with Active Site Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Na309 b:24.5 occ:1.00 O A:HOH488 2.7 32.8 1.0 O A:HOH615 2.9 25.1 1.0 O A:HOH659 3.0 30.4 1.0 N A:TRP237 3.0 12.7 1.0 CA A:TYR234 3.4 11.7 1.0 O A:GLU233 3.4 14.1 1.0 CB A:TRP237 3.5 12.4 1.0 C A:TYR234 3.5 12.3 1.0 N A:ASP236 3.5 14.4 1.0 CB A:ASP236 3.5 17.2 1.0 O A:HOH558 3.7 26.4 1.0 O A:TYR234 3.7 12.3 1.0 CA A:TRP237 3.8 12.4 1.0 CA A:ASP236 3.8 15.1 1.0 C A:ASP236 3.9 13.4 1.0 N A:VAL235 4.1 13.2 1.0 O A:HOH676 4.1 26.4 1.0 C A:GLU233 4.1 11.7 1.0 N A:TYR234 4.2 11.2 1.0 C A:VAL235 4.4 14.1 1.0 CB A:TYR234 4.5 11.8 1.0 O A:HOH620 4.5 24.7 1.0 CG A:ASP236 4.5 19.7 1.0 CD1 A:TYR234 4.8 12.2 1.0 CG A:TRP237 4.8 12.5 1.0 CA A:VAL235 4.9 13.7 1.0 CG A:TYR234 5.0 11.1 1.0 OD2 A:ASP236 5.0 23.7 1.0

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