Magnesium in PDB 3uxl: P. Putida Mandelate Racemase Co-Crystallized with the Intermediate Analogue Cupferron

All present enzymatic activity of P. Putida Mandelate Racemase Co-Crystallized with the Intermediate Analogue Cupferron:
5.1.2.2;

The structure of P. Putida Mandelate Racemase Co-Crystallized with the Intermediate Analogue Cupferron, PDB code: 3uxl was solved by A.D.Lietzan, E.Pellmann, M.St Maurice, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.20
Space group	I 4
Cell size a, b, c (Å), α, β, γ (°)	148.256, 148.256, 175.388, 90.00, 90.00, 90.00
R / Rfree (%)	18.2 / 22.7

The binding sites of Magnesium atom in the P. Putida Mandelate Racemase Co-Crystallized with the Intermediate Analogue Cupferron (pdb code 3uxl). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the P. Putida Mandelate Racemase Co-Crystallized with the Intermediate Analogue Cupferron, PDB code: 3uxl:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the P. Putida Mandelate Racemase Co-Crystallized with the Intermediate Analogue Cupferron


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of P. Putida Mandelate Racemase Co-Crystallized with the Intermediate Analogue Cupferron within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg360 b:13.8 occ:1.00 O04 A:CFI361 1.9 28.8 1.0 OE1 A:GLU221 2.0 19.1 1.0 O A:HOH518 2.1 14.2 1.0 OE1 A:GLU247 2.2 17.3 1.0 O01 A:CFI361 2.2 24.9 1.0 OD2 A:ASP195 2.2 14.2 1.0 N03 A:CFI361 2.7 33.9 1.0 N02 A:CFI361 2.8 29.4 0.5 CD A:GLU247 2.9 17.4 1.0 OE2 A:GLU247 3.0 17.6 1.0 CD A:GLU221 3.2 17.8 1.0 CG A:ASP195 3.2 16.6 1.0 OD1 A:ASP195 3.6 17.3 1.0 NZ A:LYS166 3.8 19.0 1.0 CG A:GLU221 3.9 16.2 1.0 ND2 A:ASN197 4.0 17.0 1.0 NZ A:LYS164 4.0 17.3 1.0 OE2 A:GLU221 4.1 18.0 1.0 C05 A:CFI361 4.1 37.1 1.0 O A:HOH384 4.2 16.4 1.0 NE2 A:HIS297 4.3 18.3 1.0 CD2 A:HIS297 4.3 17.4 1.0 CG A:GLU247 4.4 15.1 1.0 OE1 A:GLU222 4.4 17.3 1.0 CB A:ASP195 4.5 17.1 1.0 CE A:MET268 4.5 14.8 1.0 CE A:LYS164 4.6 16.0 1.0 C06 A:CFI361 4.8 41.0 1.0 O A:HOH591 4.9 37.2 1.0 CG A:ASN197 4.9 18.1 1.0 CB A:GLU247 5.0 16.7 1.0

Magnesium binding site 2 out of 4 in the P. Putida Mandelate Racemase Co-Crystallized with the Intermediate Analogue Cupferron


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of P. Putida Mandelate Racemase Co-Crystallized with the Intermediate Analogue Cupferron within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg360 b:15.1 occ:1.00 O04 B:CFI361 1.8 29.9 1.0 OE2 B:GLU221 2.0 19.1 1.0 O B:HOH520 2.1 17.4 1.0 OE1 B:GLU247 2.2 19.1 1.0 O01 B:CFI361 2.2 25.5 1.0 OD1 B:ASP195 2.3 14.8 1.0 N03 B:CFI361 2.8 34.3 1.0 N02 B:CFI361 2.9 29.5 0.5 CD B:GLU247 3.0 18.6 1.0 OE2 B:GLU247 3.1 18.9 1.0 CD B:GLU221 3.1 18.1 1.0 CG B:ASP195 3.2 17.6 1.0 OD2 B:ASP195 3.5 18.2 1.0 NZ B:LYS166 3.9 19.3 1.0 CG B:GLU221 3.9 16.5 1.0 ND2 B:ASN197 4.0 17.7 1.0 OE1 B:GLU221 4.1 17.7 1.0 NZ B:LYS164 4.1 16.6 1.0 C05 B:CFI361 4.1 37.1 1.0 O B:HOH367 4.3 18.8 1.0 OE1 B:GLU222 4.4 18.5 1.0 NE2 B:HIS297 4.4 18.1 1.0 CD2 B:HIS297 4.4 17.2 1.0 CG B:GLU247 4.4 16.6 1.0 CB B:ASP195 4.5 17.4 1.0 CE B:MET268 4.6 14.9 1.0 CE B:LYS164 4.8 16.4 1.0 C06 B:CFI361 4.8 41.4 1.0 O B:HOH546 4.9 34.2 1.0 CG B:ASN197 4.9 18.4 1.0 O B:HOH378 4.9 18.4 1.0 CB B:GLU247 5.0 17.4 1.0 CE B:LYS166 5.0 18.9 1.0

Magnesium binding site 3 out of 4 in the P. Putida Mandelate Racemase Co-Crystallized with the Intermediate Analogue Cupferron


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of P. Putida Mandelate Racemase Co-Crystallized with the Intermediate Analogue Cupferron within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg360 b:17.1 occ:1.00 OE1 C:GLU221 1.9 24.2 1.0 O04 C:CFI361 2.1 36.2 1.0 O01 C:CFI361 2.1 32.9 1.0 O C:HOH524 2.1 17.6 1.0 OE1 C:GLU247 2.1 22.4 1.0 OD2 C:ASP195 2.2 17.6 1.0 N02 C:CFI361 2.7 36.2 0.5 N03 C:CFI361 2.8 39.6 1.0 CD C:GLU247 3.0 21.3 1.0 CD C:GLU221 3.1 23.7 1.0 CG C:ASP195 3.1 18.8 1.0 OE2 C:GLU247 3.3 23.1 1.0 OD1 C:ASP195 3.5 18.6 1.0 NZ C:LYS166 3.9 27.6 1.0 OE2 C:GLU221 4.0 23.1 1.0 CG C:GLU221 4.0 20.4 1.0 ND2 C:ASN197 4.0 21.9 1.0 NZ C:LYS164 4.1 22.6 1.0 O C:HOH383 4.2 17.9 1.0 C05 C:CFI361 4.3 41.8 1.0 OE1 C:GLU222 4.4 20.7 1.0 CB C:ASP195 4.4 19.2 1.0 CG C:GLU247 4.5 18.9 1.0 CD2 C:HIS297 4.5 18.3 1.0 NE2 C:HIS297 4.6 19.2 1.0 O C:HOH603 4.6 48.1 1.0 CE C:LYS164 4.7 20.3 1.0 CE C:MET268 4.7 18.4 1.0 CG C:ASN197 4.8 23.1 1.0 O C:HOH395 4.9 20.7 1.0

Magnesium binding site 4 out of 4 in the P. Putida Mandelate Racemase Co-Crystallized with the Intermediate Analogue Cupferron


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of P. Putida Mandelate Racemase Co-Crystallized with the Intermediate Analogue Cupferron within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg360 b:15.7 occ:1.00 OE2 D:GLU221 1.9 21.3 1.0 O04 D:CFI361 2.1 34.4 1.0 OE1 D:GLU247 2.1 21.3 1.0 O01 D:CFI361 2.1 29.2 1.0 O D:HOH525 2.1 17.3 1.0 OD2 D:ASP195 2.2 19.3 1.0 N02 D:CFI361 2.7 33.3 0.5 N03 D:CFI361 2.8 36.7 1.0 CD D:GLU247 3.0 21.8 1.0 CD D:GLU221 3.1 22.2 1.0 CG D:ASP195 3.2 19.8 1.0 OE2 D:GLU247 3.2 23.1 1.0 OD1 D:ASP195 3.5 19.1 1.0 NZ D:LYS166 3.9 27.2 1.0 CG D:GLU221 3.9 19.5 1.0 ND2 D:ASN197 4.0 19.9 1.0 OE1 D:GLU221 4.0 21.8 1.0 NZ D:LYS164 4.1 22.9 1.0 O D:HOH374 4.1 18.0 1.0 C05 D:CFI361 4.3 39.1 1.0 OE1 D:GLU222 4.3 20.4 1.0 CG D:GLU247 4.4 18.8 1.0 CD2 D:HIS297 4.5 19.9 1.0 NE2 D:HIS297 4.5 20.9 1.0 CB D:ASP195 4.5 21.0 1.0 CE D:LYS164 4.6 20.7 1.0 CE D:MET268 4.7 18.6 1.0 O D:HOH604 4.7 47.1 1.0 CG D:ASN197 4.8 22.1 1.0 O D:HOH390 4.9 23.6 1.0

A.D.Lietzan, M.Nagar, E.A.Pellmann, J.R.Bourque, S.L.Bearne, M.St Maurice. Structure of Mandelate Racemase with Bound Intermediate Analogues Benzohydroxamate and Cupferron. Biochemistry V. 51 1160 2012.
ISSN: ISSN 0006-2960
PubMed: 22264153
DOI: 10.1021/BI2018514