Magnesium in PDB 5c5h: R195K E. Coli Mene with Bound Osb-Ams

All present enzymatic activity of R195K E. Coli Mene with Bound Osb-Ams:
6.2.1.26;

The structure of R195K E. Coli Mene with Bound Osb-Ams, PDB code: 5c5h was solved by J.S.Matarlo, R.Shek, K.R.Rajashankar, P.J.Tonge, J.B.French, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.26 / 2.40
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	126.060, 126.060, 111.752, 90.00, 90.00, 120.00
R / Rfree (%)	20 / 24.7

The binding sites of Magnesium atom in the R195K E. Coli Mene with Bound Osb-Ams (pdb code 5c5h). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the R195K E. Coli Mene with Bound Osb-Ams, PDB code: 5c5h:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the R195K E. Coli Mene with Bound Osb-Ams


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of R195K E. Coli Mene with Bound Osb-Ams within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:51.7 occ:1.00 OD1 A:ASP38 2.8 36.0 1.0 OE1 A:GLN74 2.9 29.9 1.0 O A:CYS34 3.0 28.4 1.0 NE A:ARG9 3.2 32.5 1.0 CB A:CYS34 3.3 29.4 1.0 CA A:CYS34 3.4 29.6 1.0 CG A:ASP38 3.4 35.2 1.0 C A:CYS34 3.5 29.8 1.0 OD2 A:ASP38 3.6 36.8 1.0 SG A:CYS34 3.7 29.4 1.0 CD A:GLN74 3.8 30.1 1.0 CD1 A:TRP8 3.8 23.8 1.0 CG A:ARG9 3.9 31.7 1.0 NH1 A:ARG9 3.9 33.5 1.0 NE2 A:GLN74 4.0 29.5 1.0 NE1 A:TRP8 4.0 24.2 1.0 CZ A:ARG9 4.0 33.3 1.0 CD A:ARG9 4.1 32.3 1.0 CB A:VAL37 4.1 31.6 1.0 CG1 A:VAL37 4.2 31.3 1.0 N A:ASP38 4.4 33.1 1.0 NH2 A:ARG12 4.6 39.3 1.0 CB A:ASP38 4.7 35.1 1.0 N A:ALA35 4.7 30.0 1.0 N A:CYS34 4.8 29.2 1.0 CA A:ASP38 4.9 34.6 1.0 C A:VAL37 5.0 32.2 1.0

Magnesium binding site 2 out of 3 in the R195K E. Coli Mene with Bound Osb-Ams


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of R195K E. Coli Mene with Bound Osb-Ams within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg501 b:42.6 occ:1.00 O A:HOH602 1.8 0.5 1.0 CD A:PRO133 3.2 31.6 1.0 N A:THR134 3.2 29.9 1.0 N A:PRO133 3.3 31.3 1.0 OG1 A:THR134 3.4 29.5 1.0 CB A:PRO133 3.6 31.0 1.0 CG A:GLN132 3.6 32.6 1.0 CG2 A:THR134 3.7 30.7 1.0 CG A:PRO133 3.8 31.2 1.0 C A:GLN132 3.8 30.9 1.0 CA A:PRO133 3.8 30.8 1.0 CB A:THR134 3.9 29.9 1.0 C A:PRO133 4.0 30.6 1.0 CA A:GLN132 4.0 31.5 1.0 CA A:THR134 4.2 30.0 1.0 CB A:GLN132 4.4 31.5 1.0 O A:GLN132 4.6 30.6 1.0 CD A:GLN132 4.8 33.8 1.0 NE2 A:GLN132 4.9 34.7 1.0

Magnesium binding site 3 out of 3 in the R195K E. Coli Mene with Bound Osb-Ams


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of R195K E. Coli Mene with Bound Osb-Ams within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg502 b:18.4 occ:1.00 O B:HOH721 2.9 27.4 1.0 N B:ASN61 3.4 22.9 1.0 CG B:ASN61 3.4 23.1 1.0 OD1 B:ASN61 3.5 22.8 1.0 CB B:PRO183 3.6 22.8 1.0 CB B:ASN61 3.7 23.5 1.0 CA B:PRO183 3.8 22.3 1.0 ND2 B:ASN61 3.8 22.1 1.0 CE3 B:TRP60 3.9 29.1 1.0 CG B:PRO183 3.9 22.5 1.0 CE2 B:PHE185 4.1 27.5 1.0 CA B:ASN61 4.1 23.3 1.0 CA B:TRP60 4.2 24.8 1.0 C B:TRP60 4.3 23.8 1.0 CB B:TRP60 4.3 25.7 1.0 CZ B:PHE185 4.4 27.0 1.0 N B:PRO183 4.4 22.4 1.0 O B:HOH646 4.7 27.5 1.0 CZ3 B:TRP60 4.7 29.2 1.0 O B:HOH621 4.7 29.9 1.0 CD B:PRO183 4.7 22.8 1.0 CD2 B:TRP60 4.8 27.5 1.0

J.S.Matarlo, C.E.Evans, I.Sharma, L.J.Lavaud, S.C.Ngo, R.Shek, K.R.Rajashankar, J.B.French, D.S.Tan, P.J.Tonge. Mechanism of Mene Inhibition By Acyl-Adenylate Analogues and Discovery of Novel Antibacterial Agents. Biochemistry V. 54 6514 2015.
ISSN: ISSN 0006-2960
PubMed: 26394156
DOI: 10.1021/ACS.BIOCHEM.5B00966