Calcium in PDB 7zzn: Crystal Structure of Poplar Glutathione Transferase U20

All present enzymatic activity of Crystal Structure of Poplar Glutathione Transferase U20:
2.5.1.18;

The structure of Crystal Structure of Poplar Glutathione Transferase U20, PDB code: 7zzn was solved by C.Didierjean, F.Favier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.67 / 2.01
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	55.98, 55.98, 183.15, 90, 90, 90
R / Rfree (%)	22.9 / 25.4

The binding sites of Calcium atom in the Crystal Structure of Poplar Glutathione Transferase U20 (pdb code 7zzn). 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 Crystal Structure of Poplar Glutathione Transferase U20, PDB code: 7zzn:

Calcium binding site 1 out of 1 in the Crystal Structure of Poplar Glutathione Transferase U20


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Poplar Glutathione Transferase U20 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca301 b:69.3 occ:1.00 O A:LEU174 2.3 48.8 1.0 O A:HOH409 2.3 51.2 1.0 O A:HOH434 2.6 54.3 1.0 C A:LEU174 3.5 48.3 1.0 NE2 A:HIS183 3.6 49.0 1.0 CD2 A:HIS183 3.8 48.1 1.0 CB A:LEU174 4.3 48.9 1.0 CA A:LEU174 4.4 48.6 1.0 O A:HOH413 4.4 54.1 1.0 O A:HOH485 4.4 63.0 1.0 OE1 A:GLU166 4.5 69.0 1.0 N A:GLU175 4.5 47.1 1.0 OE2 A:GLU166 4.5 70.7 1.0 CG A:GLU163 4.6 63.8 1.0 CG A:LEU174 4.6 50.2 1.0 OE2 A:GLU163 4.7 76.5 1.0 CA A:GLU175 4.7 45.7 1.0 N A:LEU174 4.8 48.9 1.0 CD A:GLU166 4.9 67.8 1.0 CE1 A:HIS183 5.0 48.7 1.0

E.Sylvestre-Gonon, L.Morette, M.Viloria, S.Mathiot, A.Boutilliat, F.Favier, N.Rouhier, C.Didierjean, A.Hecker. Biochemical and Structural Insights on the Poplar Tau Glutathione Transferase GSTU19 and 20 Paralogs Binding Flavonoids. Front Mol Biosci V. 9 58586 2022.
ISSN: ESSN 2296-889X
PubMed: 36032685
DOI: 10.3389/FMOLB.2022.958586