Calcium in PDB 3n9j: Structure of Human Glutathione Transferase Pi Class in Complex with Ethacraplatin

All present enzymatic activity of Structure of Human Glutathione Transferase Pi Class in Complex with Ethacraplatin:
2.5.1.18;

The structure of Structure of Human Glutathione Transferase Pi Class in Complex with Ethacraplatin, PDB code: 3n9j was solved by L.J.Parker, M.W.Parker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.28 / 1.85
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	76.806, 89.994, 68.870, 90.00, 98.24, 90.00
R / Rfree (%)	17.8 / 21.8

The structure of Structure of Human Glutathione Transferase Pi Class in Complex with Ethacraplatin also contains other interesting chemical elements:

Platinum	(Pt)	1 atom
Chlorine	(Cl)	5 atoms

The binding sites of Calcium atom in the Structure of Human Glutathione Transferase Pi Class in Complex with Ethacraplatin (pdb code 3n9j). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Structure of Human Glutathione Transferase Pi Class in Complex with Ethacraplatin, PDB code: 3n9j:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the Structure of Human Glutathione Transferase Pi Class in Complex with Ethacraplatin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Human Glutathione Transferase Pi Class in Complex with Ethacraplatin within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca212 b:29.1 occ:0.50 OE1 B:GLN64 2.4 17.5 1.0 OD2 A:ASP98 2.6 19.6 1.0 OD1 A:ASP98 2.6 21.4 1.0 CG A:ASP98 3.0 18.3 1.0 CD B:GLN64 3.4 15.9 1.0 NE2 B:GLN64 3.6 16.4 1.0 O B:HOH313 3.9 17.8 1.0 O B:HOH229 4.3 33.0 1.0 O A:ASP94 4.5 13.4 1.0 CB A:ASP98 4.5 16.1 1.0 O B:HOH374 4.5 39.1 1.0 O B:HOH219 4.6 15.4 1.0 NE2 B:GLN51 4.7 25.7 1.0 CG B:GLN64 4.7 14.6 1.0 O A:HOH353 4.8 28.3 1.0 OE2 B:GLU97 4.9 21.2 1.0 CB A:ASP94 5.0 14.3 1.0

Calcium binding site 2 out of 3 in the Structure of Human Glutathione Transferase Pi Class in Complex with Ethacraplatin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of Human Glutathione Transferase Pi Class in Complex with Ethacraplatin within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca211 b:23.9 occ:0.70 O B:HOH387 2.1 21.2 1.0 O B:HOH242 2.4 30.4 1.0 O B:GLY77 2.4 16.9 1.0 O B:HOH217 2.5 27.6 1.0 OE1 B:GLN147 2.6 33.8 1.0 O B:HOH243 2.8 41.9 1.0 O B:HOH226 2.9 23.4 1.0 C B:GLY77 3.6 16.6 1.0 CD B:GLN147 3.8 30.2 1.0 CB B:GLN147 4.2 18.5 1.0 CA B:GLY77 4.4 16.9 1.0 CD2 B:LEU78 4.5 13.7 1.0 O B:HOH319 4.5 32.5 1.0 O B:HOH404 4.5 30.4 1.0 N B:LEU78 4.6 16.3 1.0 CG B:GLN147 4.6 23.3 1.0 O B:HOH320 4.7 34.6 1.0 O B:ILE148 4.7 14.5 1.0 O B:HOH325 4.7 14.8 1.0 O B:LEU76 4.8 16.4 1.0 NE2 B:GLN147 4.8 32.7 1.0 O B:HOH260 4.8 17.5 1.0 CA B:LEU78 4.8 15.5 1.0

Calcium binding site 3 out of 3 in the Structure of Human Glutathione Transferase Pi Class in Complex with Ethacraplatin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Structure of Human Glutathione Transferase Pi Class in Complex with Ethacraplatin within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca213 b:20.7 occ:0.60 O A:HOH311 2.3 27.6 1.0 O B:HOH376 2.4 44.3 1.0 OE1 A:GLN64 2.4 21.6 1.0 OD2 B:ASP98 2.6 17.2 1.0 OD1 B:ASP98 2.7 21.0 1.0 CG B:ASP98 3.0 17.1 1.0 CD A:GLN64 3.4 19.0 1.0 O B:HOH354 3.5 26.4 1.0 NE2 A:GLN64 3.8 18.5 1.0 O A:HOH237 3.8 16.2 1.0 NE2 A:GLN51 4.4 29.9 1.0 O A:HOH225 4.4 12.0 1.0 CB B:ASP98 4.5 14.1 1.0 O B:HOH375 4.6 42.1 1.0 O B:ASP94 4.6 11.2 1.0 CG A:GLN64 4.8 14.3 1.0 OE2 A:GLU97 4.8 17.3 1.0 O A:HOH369 4.8 40.3 1.0

L.J.Parker, L.C.Italiano, C.J.Morton, N.C.Hancock, D.B.Ascher, J.B.Aitken, H.H.Harris, P.Campomanes, U.Rothlisberger, A.De Luca, M.Lo Bello, W.H.Ang, P.J.Dyson, M.W.Parker. Studies of Glutathione Transferase P1-1 Bound to A Platinum(IV)-Based Anticancer Compound Reveal the Molecular Basis of Its Activation. To Be Published.