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Calcium in PDB 1px7: A Folding Mutant of Human Class Pi Glutathione Transferase, Created By Mutating Aspartate 153 of the Wild-Type Protein to Glutamate

Enzymatic activity of A Folding Mutant of Human Class Pi Glutathione Transferase, Created By Mutating Aspartate 153 of the Wild-Type Protein to Glutamate

All present enzymatic activity of A Folding Mutant of Human Class Pi Glutathione Transferase, Created By Mutating Aspartate 153 of the Wild-Type Protein to Glutamate:
2.5.1.18;

Protein crystallography data

The structure of A Folding Mutant of Human Class Pi Glutathione Transferase, Created By Mutating Aspartate 153 of the Wild-Type Protein to Glutamate, PDB code: 1px7 was solved by G.K.-W.Kong, G.Polekhina, W.J.Mckinstry, M.W.Parker, B.Dragani, A.Aceto, D.Paludi, D.R.Principe, B.Mannervik, G.Stenberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.03
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 77.750, 89.330, 68.790, 90.00, 97.88, 90.00
R / Rfree (%) 17.7 / 21.8

Calcium Binding Sites:

The binding sites of Calcium atom in the A Folding Mutant of Human Class Pi Glutathione Transferase, Created By Mutating Aspartate 153 of the Wild-Type Protein to Glutamate (pdb code 1px7). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the A Folding Mutant of Human Class Pi Glutathione Transferase, Created By Mutating Aspartate 153 of the Wild-Type Protein to Glutamate, PDB code: 1px7:

Calcium binding site 1 out of 1 in 1px7

Go back to Calcium Binding Sites List in 1px7
Calcium binding site 1 out of 1 in the A Folding Mutant of Human Class Pi Glutathione Transferase, Created By Mutating Aspartate 153 of the Wild-Type Protein to Glutamate


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of A Folding Mutant of Human Class Pi Glutathione Transferase, Created By Mutating Aspartate 153 of the Wild-Type Protein to Glutamate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca3001

b:17.3
occ:0.50
O B:HOH3144 2.2 44.9 1.0
O B:HOH3094 2.5 28.1 1.0
O B:HOH3195 2.7 11.2 0.5
O B:HOH3201 2.8 44.3 1.0
NZ B:LYS81 3.0 37.4 1.0
OE2 B:GLU85 3.9 21.7 1.0
CE B:LYS81 4.1 34.6 1.0
O B:HOH3160 4.4 38.7 1.0
O B:HOH3089 4.4 26.4 1.0
OD2 B:ASP146 4.7 23.3 1.0

Reference:

G.K.-W.Kong, G.Polekhina, W.J.Mckinstry, M.W.Parker, B.Dragani, A.Aceto, D.Paludi, D.R.Principe, B.Mannervik, G.Stenberg. The Multi-Functional Role of A Highly Conserved Aspartic Acid Residue in Glutathione Transferase P1-1 To Be Published.
Page generated: Thu Jul 11 13:57:51 2024

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