Atomistry » Copper » PDB 1oe2-1rjp » 1r5a
Atomistry »
  Copper »
    PDB 1oe2-1rjp »
      1r5a »

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: Tue Jul 30 22:38:33 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy