Calcium in PDB 6dwq: Subtilisin Serine Protease Modified with the Protease Inhibitor Cyanobenzylsulfonylfluoride

The structure of Subtilisin Serine Protease Modified with the Protease Inhibitor Cyanobenzylsulfonylfluoride, PDB code: 6dwq was solved by M.Luo, C.N.Eaton, C.M.Phillips-Piro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.59 / 1.27
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	67.926, 67.926, 123.481, 90.00, 90.00, 120.00
R / Rfree (%)	12.2 / 14.8

The binding sites of Calcium atom in the Subtilisin Serine Protease Modified with the Protease Inhibitor Cyanobenzylsulfonylfluoride (pdb code 6dwq). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Subtilisin Serine Protease Modified with the Protease Inhibitor Cyanobenzylsulfonylfluoride, PDB code: 6dwq:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Subtilisin Serine Protease Modified with the Protease Inhibitor Cyanobenzylsulfonylfluoride


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Subtilisin Serine Protease Modified with the Protease Inhibitor Cyanobenzylsulfonylfluoride within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca315 b:11.8 occ:1.00 O A:THR78 2.3 12.9 1.0 O A:LEU74 2.3 11.9 1.0 O A:VAL80 2.3 11.1 1.0 OE1 A:GLN2 2.4 12.8 1.0 OD1 A:ASN76 2.4 13.7 1.0 OD1 A:ASP41 2.4 12.6 1.0 OD2 A:ASP41 2.5 12.3 1.0 CG A:ASP41 2.8 11.5 1.0 CG A:ASN76 3.4 14.0 1.0 CD A:GLN2 3.4 12.5 1.0 H A:ASN76 3.4 16.9 1.0 HG3 A:GLN2 3.5 15.9 1.0 C A:THR78 3.5 13.2 1.0 H A:VAL80 3.5 13.9 1.0 HD21 A:ASN76 3.5 17.5 1.0 C A:LEU74 3.5 11.3 1.0 C A:VAL80 3.5 10.9 1.0 H A:THR78 3.6 18.6 1.0 N A:VAL80 3.7 11.6 1.0 ND2 A:ASN76 3.8 14.5 1.0 HB A:THR78 3.9 20.9 1.0 CG A:GLN2 3.9 13.3 1.0 HA3 A:GLY79 4.0 15.1 1.0 N A:ASN76 4.0 14.1 1.0 HA A:ASP75 4.0 15.5 1.0 HB2 A:LEU74 4.1 14.6 1.0 HA A:LEU81 4.1 13.7 1.0 HB2 A:GLN2 4.2 16.8 1.0 C A:GLY79 4.2 11.3 1.0 HB1 A:ALA73 4.2 13.3 1.0 H A:LEU74 4.2 13.4 1.0 N A:THR78 4.3 15.5 1.0 N A:LEU74 4.3 11.1 1.0 CA A:VAL80 4.3 11.2 1.0 CA A:THR78 4.3 15.2 1.0 CA A:LEU74 4.3 11.6 1.0 CB A:ASP41 4.4 11.8 1.0 N A:GLY79 4.4 13.1 1.0 CA A:GLY79 4.4 12.6 1.0 N A:ASP75 4.4 12.2 1.0 N A:LEU81 4.5 11.0 1.0 CB A:THR78 4.6 17.4 1.0 NE2 A:GLN2 4.6 13.4 1.0 CA A:ASP75 4.6 12.9 1.0 CB A:ASN76 4.6 14.8 1.0 HD22 A:ASN76 4.6 17.5 1.0 HG22 A:THR78 4.6 20.5 1.0 CB A:GLN2 4.6 14.0 1.0 CA A:ASN76 4.7 14.9 1.0 CB A:LEU74 4.7 12.1 1.0 HE22 A:GLN2 4.7 16.1 1.0 C A:ASP75 4.7 13.8 1.0 HA A:VAL80 4.7 13.4 1.0 C A:ALA73 4.7 10.5 1.0 HB2 A:ASP41 4.7 14.2 1.0 HA A:ASP41 4.7 14.3 1.0 HG2 A:GLN2 4.8 15.9 1.0 CA A:LEU81 4.8 11.4 1.0 C A:ASN76 4.8 15.2 1.0 HB3 A:ASP41 4.8 14.2 1.0 HB2 A:LEU81 4.8 14.8 1.0 O A:ASN76 4.9 16.2 1.0 O A:GLY79 5.0 12.3 1.0 HA A:GLN2 5.0 17.3 1.0

Calcium binding site 2 out of 2 in the Subtilisin Serine Protease Modified with the Protease Inhibitor Cyanobenzylsulfonylfluoride


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Subtilisin Serine Protease Modified with the Protease Inhibitor Cyanobenzylsulfonylfluoride within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca316 b:22.6 occ:0.58 H A:ALA168 2.1 16.7 1.0 HB2 A:ALA168 2.7 17.7 1.0 HD2 A:PRO167 2.8 19.1 1.0 O A:ALA151 2.8 14.7 1.0 N A:ALA168 2.9 13.9 1.0 HB1 A:ALA150 3.0 16.3 1.0 O A:LEU125 3.0 22.3 1.0 HA3 A:GLY126 3.1 34.3 1.0 HB3 A:ALA168 3.2 17.7 1.0 N A:PRO167 3.2 15.5 1.0 C A:TYR166 3.2 14.6 1.0 CB A:ALA168 3.3 14.7 1.0 O A:TYR166 3.4 17.2 1.0 CD A:PRO167 3.4 15.9 1.0 CA A:ALA168 3.7 14.2 1.0 HB3 A:ALA150 3.7 16.3 1.0 CB A:ALA150 3.7 13.6 1.0 N08 A:SER220 3.8 22.6 0.5 O A:GLY165 3.8 16.2 1.0 HG2 A:PRO167 3.9 20.3 1.0 C A:GLY165 3.9 16.3 1.0 C A:PRO167 3.9 15.0 1.0 N A:TYR166 4.0 16.7 1.0 CA A:TYR166 4.0 15.8 1.0 C A:ALA151 4.0 12.9 1.0 HA A:TYR166 4.0 19.0 1.0 CA A:GLY126 4.0 28.6 1.0 CA A:PRO167 4.1 14.5 1.0 C A:LEU125 4.1 24.5 1.0 HA A:ALA168 4.1 17.1 1.0 HD3 A:PRO167 4.1 19.1 1.0 HB1 A:ALA168 4.2 17.7 1.0 CG A:PRO167 4.2 16.9 1.0 HA3 A:GLY165 4.2 20.5 1.0 HB2 A:ALA150 4.3 16.3 1.0 C07 A:SER220 4.3 21.1 0.5 HA2 A:GLY126 4.3 34.3 1.0 H A:TYR166 4.4 20.0 1.0 H A:ALA151 4.4 15.8 1.0 N A:ALA151 4.4 13.2 1.0 HB3 A:ALA151 4.5 18.0 1.0 N A:GLY126 4.6 27.9 1.0 HA A:ALA152 4.6 15.8 1.0 CA A:GLY165 4.6 17.1 1.0 HD12 A:LEU125 4.7 31.7 1.0 H A:LYS169 4.7 18.5 1.0 H A:LEU125 4.7 26.7 1.0 C A:ALA150 4.7 12.3 1.0 HA A:PRO167 4.8 17.4 1.0 CA A:ALA151 4.8 12.8 1.0 CA A:ALA150 4.8 12.8 1.0 CB A:PRO167 4.9 16.1 1.0 H A:GLY165 4.9 19.2 1.0 O A:MET123 4.9 15.7 0.3 H181 A:SER220 4.9 24.4 0.5 H A:GLY127 4.9 32.4 1.0 C A:ALA168 4.9 14.8 1.0 HG3 A:PRO167 5.0 20.3 1.0 O A:MET123 5.0 16.7 0.7 C A:ALA152 5.0 14.6 1.0

M.Luo, C.N.Eaton, C.M.Phillips-Piro, S.H.Brewer, E.E.Fenlon. Spectroscopic and Crystallographic Studies of Protease Active Sites To Be Published.