Calcium in PDB 2azz: Crystal Structure of Porcine Pancreatic Phospholipase A2 in Complex with Taurocholate

All present enzymatic activity of Crystal Structure of Porcine Pancreatic Phospholipase A2 in Complex with Taurocholate:
3.1.1.4;

The structure of Crystal Structure of Porcine Pancreatic Phospholipase A2 in Complex with Taurocholate, PDB code: 2azz was solved by Y.H.Pan, B.J.Bahnson, M.K.Jain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.08 / 2.20
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	68.650, 68.650, 65.586, 90.00, 90.00, 120.00
R / Rfree (%)	19.9 / 24.5

The structure of Crystal Structure of Porcine Pancreatic Phospholipase A2 in Complex with Taurocholate also contains other interesting chemical elements:

Chlorine

(Cl)

3 atoms

The binding sites of Calcium atom in the Crystal Structure of Porcine Pancreatic Phospholipase A2 in Complex with Taurocholate (pdb code 2azz). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Crystal Structure of Porcine Pancreatic Phospholipase A2 in Complex with Taurocholate, PDB code: 2azz:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the Crystal Structure of Porcine Pancreatic Phospholipase A2 in Complex with Taurocholate


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 Porcine Pancreatic Phospholipase A2 in Complex with Taurocholate within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca125 b:31.6 occ:1.00 O A:GLY30 2.2 30.1 1.0 O A:HOH144 2.3 26.6 1.0 O A:TYR28 2.3 27.8 1.0 OD1 A:ASP49 2.4 27.7 1.0 O A:HOH189 2.4 31.6 1.0 O A:GLY32 2.5 31.6 1.0 OD2 A:ASP49 2.6 29.4 1.0 CG A:ASP49 2.9 29.6 1.0 C A:GLY30 3.5 32.0 1.0 C A:TYR28 3.5 28.4 1.0 C A:GLY32 3.6 32.9 1.0 N A:GLY30 3.8 31.0 1.0 N A:GLY32 3.8 34.7 1.0 O A:HOH187 4.1 36.8 1.0 C A:LEU31 4.1 33.3 1.0 CA A:GLY32 4.2 33.3 1.0 O A:HOH190 4.2 47.7 1.0 CA A:TYR28 4.2 28.4 1.0 CA A:GLY30 4.3 31.2 1.0 CB A:ASP49 4.4 29.1 1.0 N A:LEU31 4.4 32.3 1.0 CA A:LEU31 4.5 33.8 1.0 CL A:CL128 4.5 39.3 1.0 N A:CYS29 4.5 29.4 1.0 O A:HOH170 4.6 34.8 1.0 CB A:TYR28 4.6 27.8 1.0 C A:CYS29 4.6 30.5 1.0 O A:HOH161 4.6 30.5 1.0 CA A:CYS29 4.7 30.1 1.0 O A:LEU31 4.7 32.9 1.0 N A:GLY33 4.7 33.4 1.0 CD1 A:TYR28 4.8 27.1 1.0 O A:CYS45 4.9 29.4 1.0

Calcium binding site 2 out of 3 in the Crystal Structure of Porcine Pancreatic Phospholipase A2 in Complex with Taurocholate


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Porcine Pancreatic Phospholipase A2 in Complex with Taurocholate within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca126 b:12.7 occ:0.50 O A:SER72 2.3 27.5 1.0 OE1 A:GLU71 2.4 29.2 1.0 OE1 A:GLU92 2.4 29.9 1.0 CD A:GLU92 3.3 28.0 1.0 C A:SER72 3.4 28.2 1.0 CD A:GLU71 3.4 29.5 1.0 N A:SER72 3.5 27.5 1.0 CG A:GLU92 3.8 27.2 1.0 CA A:SER72 3.9 28.2 1.0 CB A:SER72 4.1 29.5 1.0 O A:HOH148 4.1 23.2 1.0 OE2 A:GLU71 4.1 30.6 1.0 OE2 A:GLU92 4.4 29.1 1.0 C A:GLU71 4.4 28.4 1.0 CG A:GLU71 4.4 28.3 1.0 N A:TYR73 4.5 28.8 1.0 CA A:GLU71 4.8 28.3 1.0 CA A:TYR73 5.0 30.3 1.0

Calcium binding site 3 out of 3 in the Crystal Structure of Porcine Pancreatic Phospholipase A2 in Complex with Taurocholate


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Crystal Structure of Porcine Pancreatic Phospholipase A2 in Complex with Taurocholate within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca127 b:23.8 occ:0.50 O A:LYS62 2.3 38.7 1.0 CL A:CL130 2.9 63.1 1.0 CL A:CL129 3.0 65.4 1.0 O A:HOH172 3.0 38.7 1.0 C A:LYS62 3.5 39.3 1.0 CB A:LYS62 4.0 42.0 1.0 CA A:LYS62 4.2 40.6 1.0 N A:LYS62 4.2 39.9 1.0 N A:PHE63 4.5 38.0 1.0 CA A:PHE63 4.7 36.7 1.0

Y.H.Pan, B.J.Bahnson. Structural Basis For Bile Salt Inhibition of Pancreatic Phospholipase A2. J.Mol.Biol. V. 369 439 2007.
ISSN: ISSN 0022-2836
PubMed: 17434532
DOI: 10.1016/J.JMB.2007.03.034