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Chlorine in PDB 8c5d: Glutathione Transferase P1-1 From Mus Musculus

Enzymatic activity of Glutathione Transferase P1-1 From Mus Musculus

All present enzymatic activity of Glutathione Transferase P1-1 From Mus Musculus:
2.5.1.18;

Protein crystallography data

The structure of Glutathione Transferase P1-1 From Mus Musculus, PDB code: 8c5d was solved by A.C.Papageorgiou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.68 / 1.28
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.617, 77.366, 101.444, 90, 90, 90
R / Rfree (%) 17.5 / 20

Other elements in 8c5d:

The structure of Glutathione Transferase P1-1 From Mus Musculus also contains other interesting chemical elements:

Sodium (Na) 11 atoms
Calcium (Ca) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Glutathione Transferase P1-1 From Mus Musculus (pdb code 8c5d). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Glutathione Transferase P1-1 From Mus Musculus, PDB code: 8c5d:

Chlorine binding site 1 out of 1 in 8c5d

Go back to Chlorine Binding Sites List in 8c5d
Chlorine binding site 1 out of 1 in the Glutathione Transferase P1-1 From Mus Musculus


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Glutathione Transferase P1-1 From Mus Musculus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl511

b:26.6
occ:0.73
HH11 A:ARG186 2.4 35.0 1.0
HG2 A:ARG182 2.9 38.2 1.0
HD2 A:ARG186 3.0 30.1 1.0
O A:HOH681 3.1 28.6 1.0
O A:HOH736 3.2 39.4 1.0
NH1 A:ARG186 3.2 29.2 1.0
HE1 A:PHE142 3.3 29.6 1.0
HZ A:PHE142 3.3 29.8 1.0
HG2 A:ARG186 3.4 29.8 1.0
HG3 A:ARG186 3.5 29.8 1.0
HH12 A:ARG186 3.5 35.0 1.0
HD12 A:LEU183 3.6 32.1 1.0
HA A:LEU183 3.7 29.8 1.0
CG A:ARG186 3.7 24.9 1.0
CE1 A:PHE142 3.7 24.6 1.0
CZ A:PHE142 3.8 24.8 1.0
CD A:ARG186 3.8 25.1 1.0
CG A:ARG182 3.8 31.8 1.0
HG A:LEU183 3.9 29.9 1.0
HG3 A:ARG182 4.0 38.2 1.0
O A:ARG182 4.2 25.8 1.0
HE A:ARG182 4.2 35.5 1.0
HD11 A:LEU183 4.3 32.1 1.0
CZ A:ARG186 4.3 27.8 1.0
CD1 A:LEU183 4.3 26.7 1.0
C A:ARG182 4.4 25.9 1.0
NE A:ARG186 4.5 26.6 1.0
CA A:LEU183 4.5 24.9 1.0
HD3 A:ARG186 4.5 30.1 1.0
HD2 A:ARG182 4.5 37.6 1.0
N A:LEU183 4.6 24.3 1.0
CG A:LEU183 4.6 24.9 1.0
CD A:ARG182 4.6 31.3 1.0
HB3 A:ARG182 4.7 36.4 1.0
CB A:ARG182 4.8 30.3 1.0
NE A:ARG182 4.8 29.6 1.0
CD1 A:PHE142 4.9 23.2 1.0
CE2 A:PHE142 4.9 25.3 1.0
HD12 A:ILE148 4.9 27.2 1.0

Reference:

O.Kupreienko, F.Pouliou, K.Konstandinidis, I.Axarli, E.Douni, A.C.Papageorgiou, N.E.Labrou. Inhibition Analysis and High-Resolution Crystal Structure of Mus Musculus Glutathione Transferase P1-1. Biomolecules V. 13 2023.
ISSN: ESSN 2218-273X
PubMed: 37189361
DOI: 10.3390/BIOM13040613
Page generated: Tue Jul 30 07:46:11 2024

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