Calcium in PDB 6dwr: Trypsin Serine Protease Modified with the Protease Inhibitor Cyanobenzylsulfonylfluoride

All present enzymatic activity of Trypsin Serine Protease Modified with the Protease Inhibitor Cyanobenzylsulfonylfluoride:
3.4.21.4;

The structure of Trypsin Serine Protease Modified with the Protease Inhibitor Cyanobenzylsulfonylfluoride, PDB code: 6dwr 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)	43.21 / 1.32
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	54.614, 54.614, 106.267, 90.00, 90.00, 120.00
R / Rfree (%)	14.9 / 18.7

The binding sites of Calcium atom in the Trypsin Serine Protease Modified with the Protease Inhibitor Cyanobenzylsulfonylfluoride (pdb code 6dwr). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the Trypsin Serine Protease Modified with the Protease Inhibitor Cyanobenzylsulfonylfluoride, PDB code: 6dwr:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in the Trypsin 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 Trypsin Serine Protease Modified with the Protease Inhibitor Cyanobenzylsulfonylfluoride within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca305 b:20.9 occ:1.00 OE1 A:GLU75 2.3 21.4 1.0 O A:VAL80 2.3 20.8 1.0 O A:ASN77 2.3 21.4 1.0 O A:HOH470 2.4 21.6 1.0 OE2 A:GLU85 2.4 21.2 1.0 O A:HOH422 2.4 21.5 1.0 CD A:GLU75 3.4 21.1 1.0 HA A:VAL81 3.4 27.5 1.0 HG2 A:GLU85 3.4 27.8 1.0 C A:VAL80 3.4 21.0 1.0 CD A:GLU85 3.4 22.4 1.0 C A:ASN77 3.4 20.6 1.0 HA A:ILE78 3.5 25.0 1.0 H A:GLU82 3.5 27.2 1.0 H A:VAL80 3.5 25.2 1.0 HG3 A:GLU82 3.7 28.5 1.0 CG A:GLU85 3.8 23.2 1.0 OE2 A:GLU75 3.8 20.8 1.0 HG3 A:GLU85 3.8 27.8 1.0 H A:ASP76 3.9 26.6 1.0 HA A:GLU75 3.9 27.1 1.0 CA A:VAL81 4.1 22.9 1.0 N A:VAL81 4.2 21.5 1.0 N A:GLU82 4.2 22.6 1.0 HB3 A:ASN77 4.2 26.7 1.0 N A:VAL80 4.2 21.0 1.0 CA A:ILE78 4.2 20.8 1.0 H A:ASN77 4.3 26.6 1.0 N A:ILE78 4.3 21.1 1.0 HB2 A:GLU82 4.3 29.1 1.0 OE1 A:GLU82 4.3 23.9 1.0 HO2 A:EDO303 4.3 32.7 1.0 N A:ASN77 4.4 22.1 1.0 CA A:ASN77 4.4 21.5 1.0 CA A:VAL80 4.4 20.6 1.0 C A:ILE78 4.5 20.1 1.0 CG A:GLU82 4.5 23.8 1.0 O A:HOH491 4.5 21.9 1.0 N A:ASP76 4.6 22.1 1.0 HB3 A:GLU75 4.6 25.7 1.0 OE1 A:GLU85 4.6 22.8 1.0 HB A:VAL80 4.6 27.1 1.0 C A:VAL81 4.6 23.1 1.0 CG A:GLU75 4.6 20.8 1.0 CA A:GLU75 4.7 22.6 1.0 H21 A:EDO303 4.8 34.6 1.0 CB A:ASN77 4.8 22.2 1.0 CB A:GLU82 4.8 24.2 1.0 CB A:GLU75 4.9 21.4 1.0 CD A:GLU82 4.9 24.8 1.0 O A:ILE78 4.9 21.6 1.0 N A:ASN79 4.9 20.3 1.0 HG22 A:VAL81 4.9 30.0 1.0 C A:ASP76 4.9 21.6 1.0 H A:ASN79 4.9 24.4 1.0 H A:VAL81 5.0 25.9 1.0 O2 A:EDO303 5.0 27.2 1.0

Calcium binding site 2 out of 4 in the Trypsin 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 Trypsin Serine Protease Modified with the Protease Inhibitor Cyanobenzylsulfonylfluoride within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca306 b:65.7 occ:1.00 HD22 A:ASN54 3.0 43.9 1.0 HB3 A:ASN54 3.3 38.0 1.0 HD11 A:ILE243 3.4 33.3 0.4 HD12 A:ILE243 3.6 33.3 0.4 CD1 A:ILE243 3.8 27.8 0.4 HD13 A:ILE243 3.8 33.3 0.4 ND2 A:ASN54 3.8 36.6 1.0 O A:HOH608 3.8 48.9 1.0 O A:ILE53 3.9 31.1 1.0 O A:HOH413 4.0 35.9 1.0 CB A:ASN54 4.2 31.6 1.0 HD21 A:ASN54 4.3 43.9 1.0 HD12 A:ILE53 4.4 39.1 1.0 HD12 A:LEU128 4.5 42.1 1.0 O A:HOH500 4.5 36.8 1.0 HD12 A:ILE243 4.5 31.9 0.6 CG A:ASN54 4.5 33.1 1.0 HB A:ILE53 4.6 34.2 1.0 HB2 A:ASN54 4.6 38.0 1.0 HD13 A:ILE243 4.7 31.9 0.6 C A:ILE53 4.8 30.0 1.0 HG21 A:ILE243 4.8 32.1 0.6 HD11 A:LEU128 4.9 42.1 1.0 HG2 A:LYS240 4.9 36.5 1.0 HG A:LEU128 5.0 40.1 1.0

Calcium binding site 3 out of 4 in the Trypsin 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 3 of Trypsin Serine Protease Modified with the Protease Inhibitor Cyanobenzylsulfonylfluoride within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca307 b:69.5 occ:0.78 HG3 A:GLN197 2.0 34.1 0.4 CD A:GLN197 2.7 33.4 0.4 CG A:GLN197 2.7 28.4 0.4 O A:HOH504 2.8 45.9 1.0 OE1 A:GLN197 3.1 35.6 0.4 NE2 A:GLN197 3.1 35.0 0.4 HG2 A:GLN197 3.1 34.1 0.4 HB3 A:GLN197 3.2 34.0 0.6 H A:GLY198 3.3 27.6 1.0 HE21 A:GLN197 3.3 42.1 0.4 HG3 A:GLN197 3.6 36.5 0.6 HE22 A:GLN197 3.6 42.1 0.4 C03 A:SER200 3.7 31.9 0.8 O01 A:SER200 3.7 33.2 0.8 O18 A:SER200 3.7 35.2 0.8 N A:GLY198 3.8 23.0 1.0 O A:HOH601 3.8 51.5 1.0 C04 A:SER200 3.9 31.1 0.8 S02 A:SER200 3.9 32.5 0.8 CB A:GLN197 4.0 28.3 0.6 CB A:GLN197 4.0 27.2 0.4 H171 A:SER200 4.0 37.3 0.8 CG A:GLN197 4.1 30.4 0.6 HA A:GLN197 4.1 30.1 0.4 HA A:GLN197 4.1 30.1 0.6 HG2 A:GLN197 4.1 36.5 0.6 C10 A:SER200 4.1 35.5 0.8 HA2 A:GLY198 4.1 27.7 1.0 HB2 A:GLN197 4.2 32.7 0.4 C A:GLN197 4.4 23.6 0.6 CA A:GLN197 4.4 25.0 0.6 CA A:GLN197 4.4 25.1 0.4 C A:GLN197 4.4 24.0 0.4 H051 A:SER200 4.4 42.6 0.8 C05 A:SER200 4.5 31.9 0.8 CA A:GLY198 4.5 23.1 1.0 HH A:TYR154 4.5 48.7 1.0 C09 A:SER200 4.7 35.3 0.8 HB3 A:GLN197 4.7 32.7 0.4 HB2 A:GLN197 4.8 34.0 0.6 C06 A:SER200 4.8 35.0 0.8 HA3 A:GLY198 5.0 27.7 1.0 H181 A:SER200 5.0 38.3 0.8

Calcium binding site 4 out of 4 in the Trypsin 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 4 of Trypsin Serine Protease Modified with the Protease Inhibitor Cyanobenzylsulfonylfluoride within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca308 b:92.9 occ:1.00 HD21 A:ASN100 3.0 34.7 1.0 O A:HOH414 3.2 29.6 1.0 HG21 A:THR103 3.2 30.0 1.0 H12 A:EDO304 3.4 53.3 1.0 ND2 A:ASN100 3.4 28.9 1.0 HD22 A:ASN100 3.5 34.7 1.0 HG23 A:THR103 3.6 30.0 1.0 CG2 A:THR103 3.9 24.9 1.0 CG A:ASN100 4.3 25.7 1.0 HG22 A:THR103 4.4 30.0 1.0 C1 A:EDO304 4.4 44.4 1.0 HG1 A:THR103 4.4 26.5 1.0 OD1 A:ASN100 4.7 25.7 1.0 H11 A:EDO304 4.7 53.3 1.0 HO1 A:EDO304 4.7 45.0 1.0 O A:HOH576 4.9 29.4 1.0 HB2 A:ASN102 4.9 33.1 1.0 OG1 A:THR103 4.9 22.1 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.