Magnesium in PDB 2we5: Carbamate Kinase From Enterococcus Faecalis Bound to Mgadp

All present enzymatic activity of Carbamate Kinase From Enterococcus Faecalis Bound to Mgadp:
2.7.2.2;

The structure of Carbamate Kinase From Enterococcus Faecalis Bound to Mgadp, PDB code: 2we5 was solved by S.Ramon-Maiques, A.Marina, V.Rubio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.39
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	103.522, 103.522, 155.414, 90.00, 90.00, 120.00
R / Rfree (%)	20.1 / 21

The binding sites of Magnesium atom in the Carbamate Kinase From Enterococcus Faecalis Bound to Mgadp (pdb code 2we5). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Carbamate Kinase From Enterococcus Faecalis Bound to Mgadp, PDB code: 2we5:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Carbamate Kinase From Enterococcus Faecalis Bound to Mgadp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Carbamate Kinase From Enterococcus Faecalis Bound to Mgadp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1312 b:16.9 occ:1.00 O A:HOH2255 2.1 20.1 1.0 O A:HOH2257 2.1 16.6 1.0 O2A A:ADP1311 2.1 17.1 1.0 O A:HOH2306 2.1 18.7 1.0 O A:HOH2308 2.1 19.5 1.0 O1B A:ADP1311 2.1 16.1 1.0 PB A:ADP1311 3.2 15.4 1.0 PA A:ADP1311 3.3 16.6 1.0 O3A A:ADP1311 3.5 16.9 1.0 O3B A:ADP1311 3.8 16.3 1.0 O A:HOH2200 3.8 17.9 1.0 O A:HOH2302 4.0 32.3 1.0 NZ A:LYS271 4.1 15.5 1.0 O5' A:ADP1311 4.1 17.0 1.0 O A:GLY266 4.1 24.9 1.0 OXT A:ACT1313 4.3 22.5 1.0 O A:SER267 4.3 17.0 1.0 O A:ACT1313 4.3 28.7 1.0 O1A A:ADP1311 4.4 17.6 1.0 O A:HOH2307 4.4 18.2 1.0 CE A:LYS271 4.4 16.5 1.0 O2B A:ADP1311 4.5 15.5 1.0 CA A:SER267 4.5 18.9 1.0 C A:ACT1313 4.6 27.2 1.0 O A:HOH2305 4.7 29.0 1.0 CE A:LYS209 4.8 15.3 1.0 C A:SER267 4.9 16.9 1.0 OD2 A:ASP210 5.0 18.2 1.0

Magnesium binding site 2 out of 3 in the Carbamate Kinase From Enterococcus Faecalis Bound to Mgadp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Carbamate Kinase From Enterococcus Faecalis Bound to Mgadp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1312 b:18.6 occ:1.00 O B:HOH2250 2.0 19.6 1.0 O B:HOH2252 2.0 17.9 1.0 O B:HOH2282 2.1 21.1 1.0 O2A B:ADP1311 2.1 18.0 1.0 O1B B:ADP1311 2.1 18.6 1.0 O B:HOH2277 2.1 20.0 1.0 PB B:ADP1311 3.2 17.7 1.0 PA B:ADP1311 3.3 17.7 1.0 O3A B:ADP1311 3.5 18.0 1.0 O3B B:ADP1311 3.6 19.7 1.0 O B:HOH2210 3.9 21.3 1.0 O5' B:ADP1311 4.1 19.5 1.0 NZ B:LYS271 4.1 17.0 1.0 O B:HOH2103 4.2 26.2 1.0 O B:HOH2011 4.2 35.8 1.0 O B:GLY266 4.3 21.6 1.0 O B:HOH2171 4.4 23.9 1.0 O B:SER267 4.4 19.8 0.5 O B:SER267 4.4 18.6 0.5 O1A B:ADP1311 4.4 19.0 1.0 CE B:LYS271 4.5 17.5 1.0 O2B B:ADP1311 4.5 18.8 1.0 O B:HOH2281 4.5 35.4 1.0 CA B:SER267 4.6 18.2 0.5 CA B:SER267 4.6 20.6 0.5 CE B:LYS209 4.8 17.6 1.0 C B:SER267 4.9 18.1 0.5 C B:SER267 4.9 19.5 0.5

Magnesium binding site 3 out of 3 in the Carbamate Kinase From Enterococcus Faecalis Bound to Mgadp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Carbamate Kinase From Enterococcus Faecalis Bound to Mgadp within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg1312 b:24.8 occ:1.00 O C:HOH2213 1.9 26.2 1.0 O2A C:ADP1311 2.1 24.0 1.0 O C:HOH2210 2.1 27.4 1.0 O C:HOH2241 2.1 26.3 1.0 O1B C:ADP1311 2.1 21.8 1.0 O C:HOH2246 2.2 25.9 1.0 PB C:ADP1311 3.2 22.4 1.0 PA C:ADP1311 3.2 24.1 1.0 O3A C:ADP1311 3.5 23.0 1.0 O3B C:ADP1311 3.7 21.6 1.0 O C:HOH2176 3.8 26.5 1.0 O C:HOH2129 4.0 38.9 1.0 O C:HOH2015 4.0 29.5 1.0 O5' C:ADP1311 4.1 23.8 1.0 O C:HOH2245 4.1 44.5 1.0 NZ C:LYS271 4.1 22.2 1.0 O C:GLY266 4.2 31.8 1.0 O C:SER267 4.3 25.7 1.0 O1A C:ADP1311 4.4 25.3 1.0 O C:HOH2243 4.4 21.3 1.0 CE C:LYS271 4.5 22.2 1.0 O2B C:ADP1311 4.5 21.5 1.0 CA C:SER267 4.6 27.2 1.0 CE C:LYS209 4.8 20.1 1.0 C C:SER267 4.9 26.1 1.0 O C:HOH2242 5.0 30.9 1.0

S.Ramon-Maiques, A.Marina, A.Guinot, F.Gil-Ortiz, M.Uriarte, I.Fita, V.Rubio. Substrate Binding and Catalysis in Carbamate Kinase Ascertained By Crystallographic and Site- Directed Mutagenesis Studies. Movements and Significance of A Unique Globular Subdomain of This Key Enzyme For Fermentative Atp Production in Bacteria. J.Mol.Biol. V. 397 1261 2010.
ISSN: ISSN 0022-2836
PubMed: 20188742
DOI: 10.1016/J.JMB.2010.02.038