Calcium in PDB 4btt: Factor Xa in Complex with the Dual Thrombin-Fxa Inhibitor 31.

All present enzymatic activity of Factor Xa in Complex with the Dual Thrombin-Fxa Inhibitor 31.:
3.4.21.6;

The structure of Factor Xa in Complex with the Dual Thrombin-Fxa Inhibitor 31., PDB code: 4btt was solved by J.Meneyrol, M.Follmann, G.Lassalle, V.Wehner, G.Barre, T.Rousseaux, J.M.Altenburger, F.Petit, Z.Bocskei, C.Stehlin-Gaon, H.Schreuder, N.Alet, J.-P.Herault, L.Millet, F.Dol, C.Hasbrand, P.Schaeffer, F.Sadoun, S.Klieber, C.Briot, F.Bono, J.-M.Herbert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.68 / 2.59
Space group	P 32
Cell size a, b, c (Å), α, β, γ (°)	56.210, 56.210, 175.440, 90.00, 90.00, 120.00
R / Rfree (%)	19.93 / 23.61

The structure of Factor Xa in Complex with the Dual Thrombin-Fxa Inhibitor 31. also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Calcium atom in the Factor Xa in Complex with the Dual Thrombin-Fxa Inhibitor 31. (pdb code 4btt). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Factor Xa in Complex with the Dual Thrombin-Fxa Inhibitor 31., PDB code: 4btt:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Factor Xa in Complex with the Dual Thrombin-Fxa Inhibitor 31.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Factor Xa in Complex with the Dual Thrombin-Fxa Inhibitor 31. within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca1245 b:89.9 occ:0.87 O B:ASN72 2.2 43.2 1.0 OD1 B:ASP70 2.3 45.3 1.0 OE2 B:GLU80 2.6 67.6 1.0 OE1 B:GLU77 2.6 73.0 1.0 OE2 B:GLU77 2.8 73.4 1.0 O B:GLN75 2.9 48.0 1.0 CD B:GLU77 3.0 78.8 1.0 CD B:GLU80 3.0 68.9 1.0 C B:ASN72 3.3 43.5 1.0 CG B:ASP70 3.5 45.0 1.0 OE1 B:GLU80 3.5 60.5 1.0 O B:HOH2024 3.5 48.0 1.0 N B:ASN72 3.6 38.6 1.0 CA B:ASN72 3.9 38.8 1.0 CG B:GLU80 3.9 48.6 1.0 C B:GLN75 3.9 48.4 1.0 N B:ARG71 4.0 36.3 1.0 N B:GLU77 4.1 44.7 1.0 CA B:GLU76 4.2 44.8 1.0 CB B:ASN72 4.2 39.6 1.0 OE2 B:GLU76 4.2 73.7 1.0 OD2 B:ASP70 4.3 50.7 1.0 N B:THR73 4.4 40.7 1.0 CG B:GLU77 4.4 57.3 1.0 CA B:ASP70 4.4 33.7 1.0 CB B:ASP70 4.5 35.5 1.0 N B:GLU76 4.5 45.0 1.0 C B:ARG71 4.6 41.4 1.0 C B:GLU76 4.7 48.4 1.0 CA B:THR73 4.7 40.9 1.0 C B:ASP70 4.7 38.6 1.0 CA B:ARG71 4.9 36.6 1.0 CB B:GLU77 4.9 45.8 1.0

Calcium binding site 2 out of 2 in the Factor Xa in Complex with the Dual Thrombin-Fxa Inhibitor 31.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Factor Xa in Complex with the Dual Thrombin-Fxa Inhibitor 31. within 5.0Å range: probe atom residue distance (Å) B Occ F:Ca1245 b:43.9 occ:0.63 O F:ASN72 2.2 40.1 1.0 OE2 F:GLU80 2.2 62.5 1.0 OD1 F:ASP70 2.3 44.2 1.0 OE1 F:GLU80 2.7 64.2 1.0 CD F:GLU80 2.7 67.9 1.0 O F:HOH2022 2.8 40.2 1.0 O F:GLN75 3.0 45.4 1.0 C F:ASN72 3.3 40.6 1.0 CG F:ASP70 3.4 43.8 1.0 C F:GLN75 3.9 45.7 1.0 OE1 F:GLU77 3.9 68.2 1.0 OD2 F:ASP70 3.9 49.4 1.0 OE1 F:GLU76 3.9 73.9 1.0 CA F:GLU76 4.0 41.9 1.0 CA F:THR73 4.1 38.1 1.0 CG F:GLU80 4.1 45.7 1.0 N F:THR73 4.1 37.9 1.0 N F:GLU77 4.2 41.2 1.0 N F:ASN72 4.3 35.8 1.0 N F:GLU76 4.3 42.1 1.0 CA F:ASN72 4.4 35.9 1.0 O F:THR73 4.4 42.7 1.0 C F:THR73 4.4 43.0 1.0 CB F:ASP70 4.5 34.1 1.0 C F:GLU76 4.5 45.3 1.0 CG F:GLU77 4.6 53.0 1.0 CD F:GLU77 4.6 74.5 1.0 CA F:ASP70 4.8 32.3 1.0 CB F:GLU77 4.9 42.1 1.0 CB F:ASN72 4.9 36.9 1.0 N F:GLN75 4.9 41.9 1.0 N F:ARG71 4.9 33.8 1.0

J.Meneyrol, M.Follmann, G.Lassalle, V.Wehner, G.Barre, T.Rousseaux, J.Altenburger, F.Petit, Z.Bocskei, H.Schreuder, N.Alet, J.Herault, L.Millet, F.Dol, P.Florian, P.Schaeffer, F.Sadoun, S.Klieber, C.Briot, F.Bono, J.Herbert. 5-Chlorothiophene-2-Carboxylic Acid [(S)-2-[2-Methyl-3-(2- Oxopyrrolidin-1-Yl)Benzenesulfonylamino]-3-(4- Methylpiperazin-1-Yl)-3-Oxopropyl]Amide (SAR107375), A Selective and Potent Orally Active Dual Thrombin and Factor Xa Inhibitor. J.Med.Chem. V. 56 9441 2013.
ISSN: ISSN 0022-2623
PubMed: 24175584
DOI: 10.1021/JM4005835