Calcium in PDB 2zp4: Carboxylic Ester Hydrolase, Single Mutant H48N of Bovine Pancreatic PLA2 Enzyme

All present enzymatic activity of Carboxylic Ester Hydrolase, Single Mutant H48N of Bovine Pancreatic PLA2 Enzyme:
3.1.1.4;

The structure of Carboxylic Ester Hydrolase, Single Mutant H48N of Bovine Pancreatic PLA2 Enzyme, PDB code: 2zp4 was solved by S.P.Kanaujia, K.Sekar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.91 / 1.90
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	45.819, 45.819, 101.502, 90.00, 90.00, 120.00
R / Rfree (%)	17.8 / 20.1

The structure of Carboxylic Ester Hydrolase, Single Mutant H48N of Bovine Pancreatic PLA2 Enzyme also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Calcium atom in the Carboxylic Ester Hydrolase, Single Mutant H48N of Bovine Pancreatic PLA2 Enzyme (pdb code 2zp4). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Carboxylic Ester Hydrolase, Single Mutant H48N of Bovine Pancreatic PLA2 Enzyme, PDB code: 2zp4:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Carboxylic Ester Hydrolase, Single Mutant H48N of Bovine Pancreatic PLA2 Enzyme


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Carboxylic Ester Hydrolase, Single Mutant H48N of Bovine Pancreatic PLA2 Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca124 b:23.1 occ:1.00 O A:TYR28 2.3 19.1 1.0 O A:HOH225 2.4 26.8 1.0 O A:GLY32 2.4 24.9 1.0 OD2 A:ASP49 2.4 18.1 1.0 O A:GLY30 2.4 24.6 1.0 O A:HOH208 2.5 17.9 1.0 OD1 A:ASP49 2.6 21.3 1.0 CG A:ASP49 2.8 20.3 1.0 C A:TYR28 3.5 19.1 1.0 C A:GLY32 3.6 27.9 1.0 C A:GLY30 3.6 25.8 1.0 N A:GLY30 3.8 22.0 1.0 N A:GLY32 3.9 28.4 1.0 O A:HOH269 4.2 46.6 1.0 CA A:TYR28 4.2 20.7 1.0 O A:HOH212 4.2 18.3 1.0 CA A:GLY32 4.3 27.7 1.0 CB A:ASP49 4.3 17.8 1.0 C A:LEU31 4.3 28.8 1.0 O A:HOH203 4.4 21.2 1.0 CA A:GLY30 4.4 24.9 1.0 N A:CYS29 4.5 20.2 1.0 CB A:TYR28 4.6 19.9 1.0 N A:GLY33 4.6 28.6 1.0 N A:LEU31 4.6 27.6 1.0 C A:CYS29 4.6 21.4 1.0 CA A:CYS29 4.6 19.7 1.0 O A:HOH247 4.7 24.3 1.0 CA A:LEU31 4.7 29.9 1.0 O4 A:MRD401 4.7 34.2 1.0 CA A:GLY33 4.7 29.7 1.0 O A:CYS45 4.8 17.1 1.0 O A:LEU31 4.9 31.3 1.0

Calcium binding site 2 out of 2 in the Carboxylic Ester Hydrolase, Single Mutant H48N of Bovine Pancreatic PLA2 Enzyme


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Carboxylic Ester Hydrolase, Single Mutant H48N of Bovine Pancreatic PLA2 Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca125 b:33.9 occ:1.00 O A:HOH301 2.1 38.2 1.0 O A:HOH300 2.2 39.9 1.0 O A:HOH302 2.2 37.3 1.0 O A:HOH303 2.3 35.8 1.0 OXT A:CYS123 2.4 38.1 1.0 O A:CYS123 2.7 35.9 1.0 C A:CYS123 2.9 35.0 1.0 CA A:CYS123 4.4 34.2 1.0 O A:HOH330 4.5 47.9 1.0 CA A:GLY35 4.8 23.8 1.0

S.P.Kanaujia, K.Sekar. Structures and Molecular-Dynamics Studies of Three Active-Site Mutants of Bovine Pancreatic Phospholipase A(2) Acta Crystallogr.,Sect.D V. 64 1003 2008.
ISSN: ISSN 0907-4449
PubMed: 18931407
DOI: 10.1107/S0907444908022713