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Copper in PDB 1r5a: Glutathione S-Transferase

Enzymatic activity of Glutathione S-Transferase

All present enzymatic activity of Glutathione S-Transferase:
2.5.1.18;

Protein crystallography data

The structure of Glutathione S-Transferase, PDB code: 1r5a was solved by A.J.Oakley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.50
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 122.129, 122.129, 74.699, 90.00, 90.00, 90.00
R / Rfree (%) 23.3 / 26.5

Copper Binding Sites:

The binding sites of Copper atom in the Glutathione S-Transferase (pdb code 1r5a). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Glutathione S-Transferase, PDB code: 1r5a:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 1r5a

Go back to Copper Binding Sites List in 1r5a
Copper binding site 1 out of 3 in the Glutathione S-Transferase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Glutathione S-Transferase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1001

b:44.9
occ:0.50
NE2 A:HIS60 1.9 44.4 1.0
N A:THR2 2.5 48.8 1.0
O A:THR2 2.7 49.3 1.0
CE1 A:HIS60 2.7 43.8 1.0
CD2 A:HIS60 3.0 43.7 1.0
C A:THR2 3.3 48.7 1.0
CA A:THR2 3.5 49.2 1.0
ND1 A:HIS60 3.9 43.6 1.0
CG A:HIS60 4.1 42.7 1.0
OG1 A:THR2 4.1 49.8 1.0
O A:HOH1013 4.2 38.1 1.0
CB A:THR2 4.4 48.9 1.0
N A:THR3 4.5 47.7 1.0
CG2 A:THR2 4.9 49.2 1.0

Copper binding site 2 out of 3 in 1r5a

Go back to Copper Binding Sites List in 1r5a
Copper binding site 2 out of 3 in the Glutathione S-Transferase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Glutathione S-Transferase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1002

b:54.0
occ:0.50
NZ A:LYS144 3.1 45.8 1.0
CE A:LYS144 3.2 44.5 1.0
NH1 A:ARG180 3.7 49.7 1.0
CD A:LYS144 4.4 42.9 1.0
CZ A:ARG180 4.4 49.4 1.0
CD A:ARG180 4.6 48.6 1.0
NE A:ARG180 4.8 49.0 1.0
CG A:LYS144 4.8 41.6 1.0

Copper binding site 3 out of 3 in 1r5a

Go back to Copper Binding Sites List in 1r5a
Copper binding site 3 out of 3 in the Glutathione S-Transferase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Glutathione S-Transferase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1003

b:52.5
occ:0.50
O A:GLU193 3.1 58.6 1.0
CA A:GLY196 3.4 56.6 1.0
N A:GLY196 3.6 58.4 1.0
C A:GLY196 3.6 55.5 1.0
N A:TYR197 3.7 54.5 1.0
N A:LYS198 3.8 56.6 1.0
CB A:LYS198 3.9 58.4 1.0
N A:GLU199 3.9 57.3 1.0
C A:GLU193 4.3 58.9 1.0
CB A:GLU199 4.3 59.2 1.0
CA A:LYS198 4.3 57.7 1.0
O A:GLY196 4.4 55.2 1.0
C A:TYR197 4.6 55.1 1.0
CA A:TYR197 4.7 54.3 1.0
C A:LYS198 4.7 57.8 1.0
CA A:GLU199 4.8 57.1 1.0
OE1 A:GLU199 4.8 62.3 1.0
C A:HIS195 4.9 59.5 1.0

Reference:

R.Udomsinprasert, S.Pongjaroenkit, J.Wongsantichon, A.J.Oakley, L.A.Prapanthadara, M.C.Wilce, A.J.Ketterman. Identification, Characterization and Structure of A New Delta Class Glutathione Transferase Isoenzyme. Biochem.J. V. 388 763 2005.
ISSN: ISSN 0264-6021
PubMed: 15717864
DOI: 10.1042/BJ20042015
Page generated: Wed Oct 28 14:16:51 2020
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