Magnesium in PDB 5f05: Crystal Structure of Glutathione Transferase F5 From Populus Trichocarpa

The structure of Crystal Structure of Glutathione Transferase F5 From Populus Trichocarpa, PDB code: 5f05 was solved by C.Didierjean, N.Rouhier, H.Pegeot, F.Gense, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.35 / 1.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	54.459, 85.952, 88.520, 90.00, 97.93, 90.00
R / Rfree (%)	14.4 / 18.1

The binding sites of Magnesium atom in the Crystal Structure of Glutathione Transferase F5 From Populus Trichocarpa (pdb code 5f05). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Glutathione Transferase F5 From Populus Trichocarpa, PDB code: 5f05:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Glutathione Transferase F5 From Populus Trichocarpa


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Glutathione Transferase F5 From Populus Trichocarpa within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg303 b:20.8 occ:1.00 O A:HOH443 2.1 17.4 1.0 O A:HOH555 2.1 16.1 1.0 O A:HOH564 2.2 20.9 1.0 NE2 A:HIS190 2.3 12.7 1.0 CE1 A:HIS190 3.1 12.1 1.0 HE1 A:HIS190 3.1 14.5 1.0 CD2 A:HIS190 3.4 11.5 1.0 HD2 A:HIS190 3.6 13.8 1.0 HA A:SER152 3.9 8.7 1.0 O A:HOH585 4.2 17.1 1.0 O A:HOH589 4.2 30.4 1.0 HB3 A:SER152 4.2 11.7 1.0 ND1 A:HIS190 4.3 12.2 1.0 CG A:HIS190 4.5 8.5 1.0 O A:SER152 4.5 11.4 1.0 O A:HOH508 4.6 26.5 1.0 CA A:SER152 4.7 7.2 1.0 O A:HOH577 4.8 20.2 1.0 CB A:SER152 4.8 9.8 1.0 OG A:SER152 4.9 9.8 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Glutathione Transferase F5 From Populus Trichocarpa


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Glutathione Transferase F5 From Populus Trichocarpa within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg305 b:22.2 occ:1.00 O B:HOH549 2.0 22.4 1.0 O B:HOH439 2.1 18.3 1.0 NE2 B:HIS190 2.4 11.3 1.0 CE1 B:HIS190 3.3 13.4 1.0 CD2 B:HIS190 3.4 11.6 1.0 HE1 B:HIS190 3.5 16.1 1.0 HD2 B:HIS190 3.5 13.9 1.0 HA B:SER152 3.9 13.8 1.0 HB3 B:SER152 4.1 13.7 1.0 O B:HOH586 4.2 20.5 1.0 O B:SER152 4.3 13.4 1.0 ND1 B:HIS190 4.5 13.0 1.0 CG B:HIS190 4.5 11.0 1.0 CA B:SER152 4.7 11.5 1.0 CB B:SER152 4.7 11.4 1.0 O B:HOH559 4.7 32.0 1.0 O B:HOH564 4.8 24.2 1.0 OG B:SER152 4.9 13.9 1.0

H.Pegeot, S.Mathiot, T.Perrot, F.Gense, A.Hecker, C.Didierjean, N.Rouhier. Structural Plasticity Among Glutathione Transferase Phi Members: Natural Combination of Catalytic Residues Confers Dual Biochemical Activities. Febs J. V. 284 2442 2017.
ISSN: ISSN 1742-4658
PubMed: 28622459
DOI: 10.1111/FEBS.14138