Magnesium in PDB 7l0a: Crystal Structure of S-Formylglutathione Hydrolase (Frmb) From Staphylococcus Aureus, Apoenzyme

All present enzymatic activity of Crystal Structure of S-Formylglutathione Hydrolase (Frmb) From Staphylococcus Aureus, Apoenzyme:
3.1.2.12;

The structure of Crystal Structure of S-Formylglutathione Hydrolase (Frmb) From Staphylococcus Aureus, Apoenzyme, PDB code: 7l0a was solved by J.J.Miller, J.M.Jez, A.R.Odom John, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.81 / 1.60
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	128.303, 80.500, 66.651, 90.00, 113.84, 90.00
R / Rfree (%)	15.7 / 17.7

The binding sites of Magnesium atom in the Crystal Structure of S-Formylglutathione Hydrolase (Frmb) From Staphylococcus Aureus, Apoenzyme (pdb code 7l0a). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of S-Formylglutathione Hydrolase (Frmb) From Staphylococcus Aureus, Apoenzyme, PDB code: 7l0a:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Crystal Structure of S-Formylglutathione Hydrolase (Frmb) From Staphylococcus Aureus, Apoenzyme


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 S-Formylglutathione Hydrolase (Frmb) From Staphylococcus Aureus, Apoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:19.1 occ:1.00 H A:LEU47 2.3 24.9 1.0 H A:MET121 2.5 21.6 1.0 HD22 A:ASN151 2.6 38.2 1.0 HB2 A:MET121 2.9 27.9 1.0 HG2 A:MET121 3.0 31.3 1.0 OG A:SER120 3.0 22.6 1.0 HB3 A:SER120 3.0 22.9 1.0 O A:HOH429 3.2 39.5 1.0 HG A:SER120 3.2 27.1 1.0 HB2 A:LEU47 3.2 26.9 1.0 N A:LEU47 3.2 20.8 1.0 N A:MET121 3.3 18.0 1.0 ND2 A:ASN151 3.4 31.8 1.0 HA3 A:GLY46 3.4 20.1 1.0 HG A:LEU47 3.5 28.8 1.0 CG A:MET121 3.5 26.1 1.0 CB A:SER120 3.5 19.1 1.0 CB A:MET121 3.5 23.3 1.0 HG3 A:MET121 3.6 31.3 1.0 HD21 A:ASN151 3.8 38.2 1.0 HA2 A:GLY46 3.8 20.1 1.0 CB A:LEU47 3.9 22.4 1.0 CA A:GLY46 4.0 16.8 1.0 O A:HOH592 4.0 37.5 1.0 HD12 A:LEU47 4.0 30.1 1.0 CA A:MET121 4.0 18.6 1.0 HB3 A:ASN151 4.1 44.2 1.0 CG A:LEU47 4.1 24.0 1.0 C A:GLY46 4.1 21.1 1.0 CA A:LEU47 4.1 17.0 1.0 HB2 A:SER120 4.2 22.9 1.0 HB2 A:ASN151 4.2 44.2 1.0 H A:SER48 4.3 21.6 1.0 C A:SER120 4.3 17.8 1.0 CG A:ASN151 4.4 33.9 1.0 HB3 A:MET121 4.4 27.9 1.0 CB A:ASN151 4.4 36.9 1.0 CA A:SER120 4.5 17.0 1.0 HA A:MET121 4.5 22.3 1.0 CD1 A:LEU47 4.6 25.1 1.0 HB3 A:LEU47 4.7 26.9 1.0 HG11 A:VAL146 4.8 37.5 1.0 N A:SER48 4.8 18.0 1.0 HA A:LEU47 4.8 20.4 1.0 H A:GLY122 4.9 19.7 1.0 C A:LEU47 4.9 20.5 1.0 HA A:SER120 4.9 20.4 1.0 O A:HOH526 5.0 10.1 1.0

Magnesium binding site 2 out of 3 in the Crystal Structure of S-Formylglutathione Hydrolase (Frmb) From Staphylococcus Aureus, Apoenzyme


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 S-Formylglutathione Hydrolase (Frmb) From Staphylococcus Aureus, Apoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:13.6 occ:1.00 H B:LEU47 2.4 18.4 1.0 H B:MET121 2.5 20.0 1.0 HG B:SER120 2.6 22.4 1.0 HB3 B:SER120 2.7 20.8 1.0 HG2 B:MET121 2.9 21.5 1.0 OG B:SER120 3.0 18.7 1.0 HG B:LEU47 3.1 20.6 1.0 O B:HOH572 3.2 23.7 1.0 N B:LEU47 3.2 15.3 1.0 HB2 B:LEU47 3.2 21.5 1.0 HB2 B:MET121 3.3 21.3 1.0 N B:MET121 3.3 16.6 1.0 CB B:SER120 3.3 17.4 1.0 HA3 B:GLY46 3.3 18.0 1.0 HD12 B:LEU47 3.4 24.5 1.0 O B:HOH540 3.4 28.1 1.0 HD22 B:LEU155 3.6 30.9 1.0 HD13 B:LEU155 3.7 27.7 1.0 CG B:MET121 3.7 17.9 1.0 HA2 B:GLY46 3.7 18.0 1.0 CG B:LEU47 3.7 17.1 1.0 CB B:LEU47 3.8 17.9 1.0 CB B:MET121 3.8 17.8 1.0 CA B:GLY46 3.9 15.0 1.0 HG3 B:MET121 3.9 21.5 1.0 CD1 B:LEU47 4.0 20.4 1.0 HB2 B:SER120 4.0 20.8 1.0 C B:GLY46 4.0 17.6 1.0 HB3 B:LEU155 4.1 28.1 1.0 CA B:LEU47 4.1 15.7 1.0 CA B:MET121 4.2 14.4 1.0 O B:HOH452 4.2 36.0 1.0 C B:SER120 4.2 18.0 1.0 CA B:SER120 4.3 20.5 1.0 HD11 B:LEU47 4.4 24.5 1.0 CD2 B:LEU155 4.5 25.8 1.0 CD1 B:LEU155 4.6 23.1 1.0 HA B:MET121 4.7 17.2 1.0 HB3 B:LEU47 4.7 21.5 1.0 HB3 B:MET121 4.7 21.3 1.0 HA B:LEU47 4.7 18.8 1.0 HD13 B:LEU47 4.8 24.5 1.0 H B:SER48 4.8 19.9 1.0 HA B:SER120 4.8 24.6 1.0 H B:GLY122 4.9 18.4 1.0 HD21 B:LEU155 4.9 30.9 1.0 HD11 B:LEU155 4.9 27.7 1.0 CG B:LEU155 4.9 26.3 1.0 H B:GLU156 4.9 27.4 1.0 HG21 B:VAL146 4.9 24.4 1.0 CB B:LEU155 4.9 23.4 1.0 NE2 B:HIS233 5.0 21.9 1.0

Magnesium binding site 3 out of 3 in the Crystal Structure of S-Formylglutathione Hydrolase (Frmb) From Staphylococcus Aureus, Apoenzyme


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of S-Formylglutathione Hydrolase (Frmb) From Staphylococcus Aureus, Apoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg302 b:15.0 occ:1.00 HE2 B:HIS119 2.5 20.4 1.0 H B:SER48 2.6 19.9 1.0 HB2 B:SER48 3.0 26.4 1.0 HG B:SER49 3.0 20.6 1.0 OG B:SER49 3.0 17.2 1.0 HA3 B:GLY46 3.1 18.0 1.0 H B:GLY46 3.2 21.0 1.0 NE2 B:HIS119 3.3 17.0 1.0 O B:HOH540 3.4 28.1 1.0 N B:SER48 3.4 16.6 1.0 C B:GLY46 3.4 17.6 1.0 CA B:GLY46 3.6 15.0 1.0 O B:HOH645 3.6 35.3 1.0 HB2 B:SER49 3.6 19.8 1.0 N B:LEU47 3.7 15.3 1.0 H B:LEU47 3.7 18.4 1.0 O B:GLY46 3.8 16.2 1.0 N B:GLY46 3.8 17.5 1.0 CB B:SER48 3.8 22.0 1.0 H B:SER49 3.8 20.1 1.0 CB B:SER49 3.9 16.5 1.0 N B:SER49 3.9 16.7 1.0 HE2 B:TYR235 3.9 16.7 1.0 CA B:SER48 3.9 17.5 1.0 HD2 B:HIS119 3.9 19.3 1.0 C B:SER48 4.0 19.1 1.0 CD2 B:HIS119 4.0 16.1 1.0 HZ3 B:TRP238 4.1 17.9 1.0 O B:HOH452 4.2 36.0 1.0 CE1 B:HIS119 4.3 16.3 1.0 OH B:TYR235 4.4 17.2 1.0 HB3 B:SER48 4.4 26.4 1.0 C B:LEU47 4.5 18.0 1.0 CA B:SER49 4.5 15.0 1.0 HA2 B:GLY46 4.5 18.0 1.0 HH B:TYR235 4.5 20.6 1.0 HE1 B:HIS119 4.5 19.5 1.0 HH2 B:TRP238 4.5 21.9 1.0 CE2 B:TYR235 4.5 13.9 1.0 CZ3 B:TRP238 4.6 14.9 1.0 OG B:SER48 4.6 27.1 1.0 O B:SER48 4.6 23.8 1.0 CA B:LEU47 4.7 15.7 1.0 HB3 B:SER49 4.7 19.8 1.0 HB2 B:HIS45 4.7 17.9 1.0 O B:HOH585 4.7 43.2 1.0 HA B:SER48 4.8 21.0 1.0 HG B:SER48 4.8 32.5 1.0 CH2 B:TRP238 4.8 18.2 1.0 CZ B:TYR235 4.8 13.7 1.0 HD1 B:HIS45 4.9 16.8 1.0 HA B:SER49 4.9 18.0 1.0

J.J.Miller, I.T.Shah, J.Hatten, Y.Barekatain, E.A.Mueller, A.M.Moustafa, R.L.Edwaards, C.S.Dowd, P.J.Planet, F.L.Muller, J.M.Jez, A.R.Odom John. Structure-Guided Microbial Targeting of Antistaphylococcal Prodrugs To Be Published.