Magnesium in PDB 4hnc: P. Putida C92S/K166C/C264S Mandelate Racemase Co-Crystallized with Benzilic Acid

All present enzymatic activity of P. Putida C92S/K166C/C264S Mandelate Racemase Co-Crystallized with Benzilic Acid:
5.1.2.2;

The structure of P. Putida C92S/K166C/C264S Mandelate Racemase Co-Crystallized with Benzilic Acid, PDB code: 4hnc was solved by A.D.Lietzan, M.St. Maurice, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.89
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	148.464, 148.464, 169.987, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 19.8

The binding sites of Magnesium atom in the P. Putida C92S/K166C/C264S Mandelate Racemase Co-Crystallized with Benzilic Acid (pdb code 4hnc). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the P. Putida C92S/K166C/C264S Mandelate Racemase Co-Crystallized with Benzilic Acid, PDB code: 4hnc:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the P. Putida C92S/K166C/C264S Mandelate Racemase Co-Crystallized with Benzilic Acid


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of P. Putida C92S/K166C/C264S Mandelate Racemase Co-Crystallized with Benzilic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:10.2 occ:1.00 OE2 A:GLU221 2.0 9.3 1.0 O01 A:0UT402 2.0 13.8 1.0 OE1 A:GLU247 2.0 10.1 1.0 O A:HOH763 2.1 11.4 1.0 OD2 A:ASP195 2.1 10.6 1.0 O05 A:0UT402 2.1 16.2 1.0 C02 A:0UT402 2.9 17.6 1.0 C04 A:0UT402 3.0 17.8 0.5 CD A:GLU247 3.0 10.6 1.0 CG A:ASP195 3.1 11.1 1.0 CD A:GLU221 3.1 9.6 1.0 OE2 A:GLU247 3.4 11.6 1.0 OD1 A:ASP195 3.4 11.1 1.0 C06 A:0UT402 3.7 21.7 1.0 CG A:GLU221 3.8 9.2 1.0 NZ A:LYS164 3.8 9.8 1.0 OE1 A:GLU221 4.0 9.8 1.0 O A:HOH518 4.1 7.8 1.0 O03 A:0UT402 4.1 17.5 1.0 OE1 A:GLU222 4.2 11.7 1.0 C07 A:0UT402 4.3 16.3 0.6 CG A:GLU247 4.4 10.0 1.0 C1 A:0UT402 4.4 25.0 1.0 C5 A:0UT402 4.4 26.4 1.0 CE A:MET268 4.4 8.3 1.0 CB A:ASP195 4.4 10.4 1.0 CE A:LYS164 4.5 10.0 1.0 CD2 A:HIS297 4.6 10.0 1.0 NE2 A:HIS297 4.7 11.0 1.0 C10 A:0UT402 4.7 16.0 0.6 OD1 A:ASN197 4.8 12.5 0.5 CB A:GLU221 4.9 8.9 1.0 CB A:GLU247 5.0 9.7 1.0

Magnesium binding site 2 out of 2 in the P. Putida C92S/K166C/C264S Mandelate Racemase Co-Crystallized with Benzilic Acid


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of P. Putida C92S/K166C/C264S Mandelate Racemase Co-Crystallized with Benzilic Acid within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg401 b:15.5 occ:1.00 OE2 B:GLU221 1.9 13.6 1.0 O03 B:0UT402 2.1 15.2 1.0 OE1 B:GLU247 2.1 13.7 1.0 OD2 B:ASP195 2.1 15.1 1.0 O05 B:0UT402 2.1 15.4 0.8 O B:HOH724 2.2 14.6 1.0 C02 B:0UT402 2.9 17.3 1.0 CD B:GLU221 3.0 13.8 1.0 C04 B:0UT402 3.0 17.2 0.5 CD B:GLU247 3.1 13.3 1.0 CG B:ASP195 3.1 16.6 1.0 OE2 B:GLU247 3.4 14.0 1.0 OD1 B:ASP195 3.4 15.8 1.0 CG B:GLU221 3.7 12.5 1.0 NZ B:LYS164 3.8 15.6 1.0 C06 B:0UT402 3.9 18.1 0.5 OE1 B:GLU221 3.9 13.9 1.0 O B:HOH517 4.1 11.6 1.0 OE1 B:GLU222 4.1 17.1 1.0 O01 B:0UT402 4.1 15.1 0.5 C5 B:0UT402 4.3 19.4 0.5 C07 B:0UT402 4.3 17.2 0.5 CG B:GLU247 4.4 12.2 1.0 CB B:ASP195 4.4 16.1 1.0 CE B:LYS164 4.5 16.7 1.0 CE B:MET268 4.5 12.1 1.0 CD2 B:HIS297 4.6 14.4 1.0 NE2 B:HIS297 4.7 14.3 1.0 OD1 B:ASN197 4.7 16.2 0.5 CB B:GLU221 4.8 13.1 1.0 C6 B:0UT402 4.8 18.3 0.5 C1 B:0UT402 4.9 19.9 0.5 CD B:GLU222 5.0 17.1 1.0 O B:HOH533 5.0 20.1 1.0

M.Nagar, A.D.Lietzan, M.St Maurice, S.L.Bearne. Potent Inhibition of Mandelate Racemase By A Fluorinated Substrate-Product Analogue with A Novel Binding Mode. Biochemistry V. 53 1169 2014.
ISSN: ISSN 0006-2960
PubMed: 24472022
DOI: 10.1021/BI401703H