Calcium in PDB 5ok8: Crystal Structure of Protein LPP20 (HP1456) From Helicobacter Pylori

The structure of Crystal Structure of Protein LPP20 (HP1456) From Helicobacter Pylori, PDB code: 5ok8 was solved by G.Zanotti, N.Mishra, F.Valesse, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.38 / 1.87
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.303, 90.424, 114.522, 90.00, 90.00, 90.00
R / Rfree (%)	22.9 / 26.8

The binding sites of Calcium atom in the Crystal Structure of Protein LPP20 (HP1456) From Helicobacter Pylori (pdb code 5ok8). 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 Crystal Structure of Protein LPP20 (HP1456) From Helicobacter Pylori, PDB code: 5ok8:

Calcium binding site 1 out of 1 in the Crystal Structure of Protein LPP20 (HP1456) From Helicobacter Pylori


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Protein LPP20 (HP1456) From Helicobacter Pylori within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca202 b:49.2 occ:1.00 O B:HOH330 2.1 34.7 1.0 O B:HOH329 2.2 41.1 1.0 O C:HOH275 2.2 40.9 1.0 O B:HOH305 2.2 40.4 1.0 OD1 B:ASP71 2.5 34.9 1.0 O C:HOH215 2.5 45.0 1.0 CG B:ASP71 3.4 37.7 1.0 OD2 B:ASP71 3.6 31.8 1.0 O C:HOH266 3.7 40.8 1.0 O B:HOH314 4.1 37.8 1.0 O C:HOH289 4.1 45.3 1.0 O B:HOH339 4.1 36.4 1.0 NZ B:LYS88 4.4 46.5 1.0 O B:HOH322 4.5 39.0 1.0 NH1 C:ARG151 4.6 40.1 1.0 O B:LEU72 4.6 28.3 1.0 OE1 C:GLU70 4.7 38.5 1.0 CB B:ASP71 4.7 31.7 1.0 OE2 C:GLU70 4.8 39.2 1.0 OE1 B:GLN84 4.8 43.4 1.0 N B:LEU72 4.9 30.0 1.0 CG B:GLN84 5.0 36.5 1.0

F.Vallese, N.M.Mishra, M.Pagliari, P.Berto, G.Codolo, M.De Bernard, G.Zanotti. Helicobacter Pylori Antigenic LPP20 Is A Structural Homologue of Tip Alpha and Promotes Epithelial-Mesenchymal Transition. Biochim. Biophys. Acta V.1861 3263 2017.
ISSN: ISSN 0006-3002
PubMed: 28947343
DOI: 10.1016/J.BBAGEN.2017.09.017