Calcium in PDB 1kp4: Calcium-Bound Form of Prokaryotic Phospholipase A2

All present enzymatic activity of Calcium-Bound Form of Prokaryotic Phospholipase A2:
3.1.1.4;

The structure of Calcium-Bound Form of Prokaryotic Phospholipase A2, PDB code: 1kp4 was solved by Y.Matoba, Y.Katsube, M.Sugiyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	5.00 / 1.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	38.280, 54.250, 30.650, 90.00, 90.20, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Calcium atom in the Calcium-Bound Form of Prokaryotic Phospholipase A2 (pdb code 1kp4). 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 Calcium-Bound Form of Prokaryotic Phospholipase A2, PDB code: 1kp4:

Calcium binding site 1 out of 1 in the Calcium-Bound Form of Prokaryotic Phospholipase A2


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Calcium-Bound Form of Prokaryotic Phospholipase A2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca200 b:24.0 occ:1.00 O A:LEU44 2.3 22.6 1.0 O A:HOH201 2.3 31.3 1.0 O A:HOH202 2.4 27.1 1.0 OD2 A:ASP43 2.4 25.0 1.0 O A:HOH203 2.4 31.5 1.0 OD1 A:ASP65 2.5 21.2 1.0 OD2 A:ASP65 2.5 23.1 1.0 CG A:ASP65 2.9 20.6 1.0 C A:LEU44 3.6 22.0 1.0 CG A:ASP43 3.6 27.7 1.0 N A:LEU44 4.1 23.2 1.0 C A:ASP43 4.2 25.2 1.0 OD1 A:ASP43 4.2 28.1 1.0 O A:HOH256 4.3 51.2 1.0 O A:HOH258 4.3 52.6 1.0 O A:HOH245 4.3 45.1 1.0 CB A:ASP65 4.4 21.2 1.0 CA A:LEU44 4.4 20.5 1.0 O A:HOH286 4.4 67.2 1.0 O A:CYS61 4.4 23.0 1.0 N A:ASP43 4.4 26.1 1.0 O A:ASP43 4.4 26.8 1.0 N A:CYS45 4.5 24.1 1.0 O A:THR46 4.6 33.1 1.0 CA A:CYS45 4.6 21.7 1.0 CA A:ASP43 4.6 24.2 1.0 N A:THR46 4.7 27.5 1.0 CB A:CYS61 4.7 21.1 1.0 CB A:ASP43 4.7 24.1 1.0 O A:HOH226 4.8 35.7 1.0 OG1 A:THR42 4.8 26.2 1.0 NH2 A:ARG69 4.9 27.8 1.0 C A:CYS45 4.9 24.0 1.0

Y.Matoba, Y.Katsube, M.Sugiyama. The Crystal Structure of Prokaryotic Phospholipase A2. J.Biol.Chem. V. 277 20059 2002.
ISSN: ISSN 0021-9258
PubMed: 11897785
DOI: 10.1074/JBC.M200263200