Calcium 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:

Magnesium	(Mg)	2 atoms
Chlorine	(Cl)	2 atoms

The binding sites of Calcium 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 Calcium atom.
In total only one binding site of Calcium was determined in the Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Maltopentaose, PDB code: 5hpo:

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


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca 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:Ca1103 b:16.1 occ:1.00 OE1 A:GLU939 2.2 17.1 1.0 OD1 A:ASP1054 2.3 17.6 1.0 O A:GLY961 2.4 18.0 1.0 O A:THR958 2.4 16.3 1.0 OE1 A:GLU941 2.4 16.5 1.0 OE2 A:GLU941 2.5 17.7 1.0 O A:ASP1054 2.6 14.8 1.0 CD A:GLU941 2.8 17.4 1.0 CD A:GLU939 3.4 16.8 1.0 CG A:ASP1054 3.5 18.2 1.0 C A:ASP1054 3.5 15.5 1.0 C A:THR958 3.5 17.9 1.0 C A:GLY961 3.5 17.8 1.0 CA A:ASP1054 3.9 16.6 1.0 OG1 A:THR958 4.0 18.1 1.0 OE2 A:GLU939 4.2 17.9 1.0 CB A:GLU939 4.2 15.3 1.0 N A:THR958 4.2 18.6 1.0 CG A:GLU939 4.2 16.2 1.0 N A:GLY961 4.3 17.7 1.0 CA A:PHE962 4.3 17.1 1.0 N A:PHE962 4.3 16.8 1.0 CB A:ASP1054 4.3 16.8 1.0 N A:GLY959 4.3 17.6 1.0 CG A:GLU941 4.3 16.7 1.0 OD2 A:ASP1054 4.4 19.5 1.0 CA A:GLY959 4.4 17.4 1.0 CA A:THR958 4.4 18.0 1.0 CA A:GLY961 4.5 18.3 1.0 CA A:GLU939 4.5 15.4 1.0 CB A:TYR957 4.6 18.9 1.0 N A:HIS1055 4.6 14.4 1.0 N A:ALA940 4.6 14.7 1.0 CB A:HIS1055 4.6 15.0 1.0 CB A:PHE962 4.7 17.1 1.0 C A:GLY959 4.8 17.4 1.0 CB A:THR958 4.8 18.4 1.0 N A:THR960 4.8 18.7 1.0 CA A:HIS1055 5.0 15.2 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