Atomistry » Calcium » PDB 2zp5-3a4h » 2zp5
Atomistry »
  Calcium »
    PDB 2zp5-3a4h »
      2zp5 »

Calcium in PDB 2zp5: Carboxylic Ester Hydrolase, Single Mutant D49K of Bovine Pancreatic PLA2 Enzyme

Enzymatic activity of Carboxylic Ester Hydrolase, Single Mutant D49K of Bovine Pancreatic PLA2 Enzyme

All present enzymatic activity of Carboxylic Ester Hydrolase, Single Mutant D49K of Bovine Pancreatic PLA2 Enzyme:
3.1.1.4;

Protein crystallography data

The structure of Carboxylic Ester Hydrolase, Single Mutant D49K of Bovine Pancreatic PLA2 Enzyme, PDB code: 2zp5 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) 23.09 / 1.90
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 46.187, 46.187, 101.920, 90.00, 90.00, 120.00
R / Rfree (%) 19.7 / 23.5

Other elements in 2zp5:

The structure of Carboxylic Ester Hydrolase, Single Mutant D49K of Bovine Pancreatic PLA2 Enzyme also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Carboxylic Ester Hydrolase, Single Mutant D49K of Bovine Pancreatic PLA2 Enzyme (pdb code 2zp5). 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 Carboxylic Ester Hydrolase, Single Mutant D49K of Bovine Pancreatic PLA2 Enzyme, PDB code: 2zp5:

Calcium binding site 1 out of 1 in 2zp5

Go back to Calcium Binding Sites List in 2zp5
Calcium binding site 1 out of 1 in the Carboxylic Ester Hydrolase, Single Mutant D49K 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 D49K of Bovine Pancreatic PLA2 Enzyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca124

b:49.3
occ:1.00
 O A:HOH325 2.0 46.2 1.0
O A:HOH323 2.2 45.6 1.0
O A:HOH322 2.2 46.5 1.0
O A:HOH324 2.3 44.0 1.0
OXT A:CYS123 2.5 48.7 1.0
C A:CYS123 3.2 47.0 1.0
O A:CYS123 3.3 47.8 1.0
CA A:CYS123 4.7 46.0 1.0
CA A:GLY35 4.8 30.7 1.0

Reference:

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
Page generated: Tue Jul 8 10:08:37 2025

Last articles

Mn in 9LJU
Mn in 9LJW
Mn in 9LJS
Mn in 9LJR
Mn in 9LJT
Mn in 9LJV
Mg in 9UA2
Mg in 9R96
Mg in 9VM1
Mg in 9P01
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy