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Osmium in PDB 8ax2: Crystal Structure of Trametes Versicolor Glutathione Transferase Omega 3S in Complex with Glutathione and Pentachloro-Nitrosyl-Osmate

Enzymatic activity of Crystal Structure of Trametes Versicolor Glutathione Transferase Omega 3S in Complex with Glutathione and Pentachloro-Nitrosyl-Osmate

All present enzymatic activity of Crystal Structure of Trametes Versicolor Glutathione Transferase Omega 3S in Complex with Glutathione and Pentachloro-Nitrosyl-Osmate:
2.5.1.18;

Protein crystallography data

The structure of Crystal Structure of Trametes Versicolor Glutathione Transferase Omega 3S in Complex with Glutathione and Pentachloro-Nitrosyl-Osmate, PDB code: 8ax2 was solved by M.Schwartz, C.Didierjean, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.57 / 1.62
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 50.615, 104.548, 108.092, 90, 90, 90
R / Rfree (%) 18.5 / 20.8

Other elements in 8ax2:

The structure of Crystal Structure of Trametes Versicolor Glutathione Transferase Omega 3S in Complex with Glutathione and Pentachloro-Nitrosyl-Osmate also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Osmium Binding Sites:

The binding sites of Osmium atom in the Crystal Structure of Trametes Versicolor Glutathione Transferase Omega 3S in Complex with Glutathione and Pentachloro-Nitrosyl-Osmate (pdb code 8ax2). This binding sites where shown within 5.0 Angstroms radius around Osmium atom.
In total 2 binding sites of Osmium where determined in the Crystal Structure of Trametes Versicolor Glutathione Transferase Omega 3S in Complex with Glutathione and Pentachloro-Nitrosyl-Osmate, PDB code: 8ax2:
Jump to Osmium binding site number: 1; 2;

Osmium binding site 1 out of 2 in 8ax2

Go back to Osmium Binding Sites List in 8ax2
Osmium binding site 1 out of 2 in the Crystal Structure of Trametes Versicolor Glutathione Transferase Omega 3S in Complex with Glutathione and Pentachloro-Nitrosyl-Osmate


Mono view


Stereo pair view

A full contact list of Osmium with other atoms in the Os binding site number 1 of Crystal Structure of Trametes Versicolor Glutathione Transferase Omega 3S in Complex with Glutathione and Pentachloro-Nitrosyl-Osmate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Os301

b:92.3
occ:0.38
 SG2 A:GSH303 2.9 30.2 0.7
HSG A:GSH303 3.8 36.2 0.7
HB22 A:GSH303 4.1 30.1 0.7
CB2 A:GSH303 4.2 25.1 0.7
CD A:PRO16 4.4 15.8 1.0
HA2 A:GSH303 4.4 27.4 0.7
CZ A:PHE128 4.6 30.6 1.0
CD1 A:PHE14 4.7 22.6 1.0
O A:HOH401 4.7 28.4 1.0
CE1 A:PHE14 4.8 27.2 1.0
CA2 A:GSH303 4.9 22.8 0.7
CG A:PRO16 4.9 16.6 1.0
HB23 A:GSH303 4.9 30.1 0.7
CE2 A:TYR17 5.0 18.9 1.0

Osmium binding site 2 out of 2 in 8ax2

Go back to Osmium Binding Sites List in 8ax2
Osmium binding site 2 out of 2 in the Crystal Structure of Trametes Versicolor Glutathione Transferase Omega 3S in Complex with Glutathione and Pentachloro-Nitrosyl-Osmate


Mono view


Stereo pair view

A full contact list of Osmium with other atoms in the Os binding site number 2 of Crystal Structure of Trametes Versicolor Glutathione Transferase Omega 3S in Complex with Glutathione and Pentachloro-Nitrosyl-Osmate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Os301

b:88.2
occ:0.28
 HSG B:GSH303 1.7 40.8 0.7
HA2 B:GSH303 2.4 31.6 0.7
SG2 B:GSH303 2.7 34.0 0.7
HB22 B:GSH303 2.9 30.5 0.7
CB2 B:GSH303 3.0 25.4 0.7
CA2 B:GSH303 3.1 26.4 0.7
HN3 B:GSH303 3.7 33.1 0.7
HB23 B:GSH303 4.0 30.5 0.7
C2 B:GSH303 4.1 22.9 0.7
N2 B:GSH303 4.1 22.8 0.7
N3 B:GSH303 4.2 27.6 0.7
OE1 B:GSH303 4.2 25.6 0.7
CE1 B:PHE14 4.3 29.3 1.0
CD1 B:GSH303 4.6 22.1 0.7
HN2 B:GSH303 4.7 27.4 0.7
CE2 B:TYR17 4.8 20.0 1.0
CD1 B:LEU40 4.9 23.8 1.0
CD2 B:TYR17 5.0 17.3 1.0

Reference:

M.Schwartz, T.Perrot, J.Beurton, F.Zannini, M.Morel-Rouhier, E.Gelhaye, F.Neiers, D.Schaniel, F.Favier, J.P.Jacquot, P.Leroy, I.Clarot, A.Boudier, C.Didierjean. Structural Insights Into the Interactions of Glutathione Transferases with A Nitric Oxide Carrier and Sodium Nitroprusside. Biochem.Biophys.Res.Commun. V. 649 79 2023.
ISSN: ESSN 1090-2104
PubMed: 36758482
DOI: 10.1016/J.BBRC.2023.01.099
Page generated: Fri Apr 7 19:37:11 2023

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