Magnesium in PDB 5hpo: Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Maltopentaose

The structure of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Maltopentaose, PDB code: 5hpo was solved by A.S.Halavaty, S.H.Light, G.Minasov, J.Winsor, S.Grimshaw, L.Shuvalova, S.Peterson, W.F.Anderson, Center For Structural Genomics Of Infectiousdiseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.92 / 1.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	162.646, 100.131, 73.281, 90.00, 105.47, 90.00
R / Rfree (%)	13.3 / 16.4

The structure of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Maltopentaose also contains other interesting chemical elements:

Chlorine	(Cl)	2 atoms
Calcium	(Ca)	1 atom

The binding sites of Magnesium atom in the Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Maltopentaose (pdb code 5hpo). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Maltopentaose, PDB code: 5hpo:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Maltopentaose


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Maltopentaose within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1101 b:24.5 occ:1.00 O A:HOH2220 2.0 23.2 1.0 O A:HOH2454 2.0 24.1 1.0 O A:HOH1989 2.1 25.4 1.0 O A:HOH2387 2.1 32.5 1.0 O A:HOH1431 2.1 21.5 1.0 O A:HOH2337 2.2 24.1 1.0 O A:HOH1485 4.0 18.1 1.0 ND2 A:ASN575 4.0 20.1 1.0 O A:HOH1877 4.2 25.3 1.0 CG A:ASN575 4.2 20.2 1.0 O A:HOH1882 4.2 41.8 1.0 OD1 A:ASN575 4.3 19.6 1.0 O A:HOH2227 4.3 36.5 1.0 OD1 A:ASP529 4.3 20.3 1.0 O A:HOH1755 4.4 32.4 1.0 O A:HOH2435 4.4 48.6 1.0 O A:GLY527 4.5 19.0 1.0 CE1 A:HIS444 4.9 20.8 1.0

Magnesium binding site 2 out of 2 in the Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Maltopentaose


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Maltopentaose within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1102 b:24.2 occ:1.00 O A:HOH1352 2.0 21.9 1.0 O A:HOH1289 2.1 22.5 1.0 O A:HOH1239 2.1 22.9 1.0 OD1 A:ASN346 2.1 19.4 1.0 O A:HOH1349 2.1 21.8 1.0 O A:HOH2260 2.1 23.9 1.0 CG A:ASN346 3.1 18.8 1.0 ND2 A:ASN346 3.4 18.4 1.0 O A:HOH1331 3.9 25.1 1.0 OD1 A:ASP342 4.1 21.6 1.0 OD2 A:ASP152 4.1 28.1 1.0 OD2 A:ASP349 4.1 23.9 1.0 OD2 A:ASP154 4.2 21.7 1.0 OD2 A:ASP342 4.2 20.4 1.0 ND2 A:ASN345 4.2 24.4 1.0 O A:HOH2311 4.2 32.2 1.0 OD1 A:ASP154 4.4 23.1 1.0 CB A:ASN346 4.4 17.6 1.0 O A:HOH1829 4.5 46.6 1.0 CG A:ASP342 4.5 20.9 1.0 CG A:ASP154 4.7 22.9 1.0 CA A:ASN346 4.8 17.7 1.0

S.H.Light, L.A.Cahoon, K.V.Mahasenan, M.Lee, B.Boggess, A.S.Halavaty, S.Mobashery, N.E.Freitag, W.F.Anderson. Transferase Versus Hydrolase: the Role of Conformational Flexibility in Reaction Specificity. Structure V. 25 295 2017.
ISSN: ISSN 1878-4186
PubMed: 28089449
DOI: 10.1016/J.STR.2016.12.007