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Calcium in PDB 1kvx: Carboxylic Ester Hydrolase, Single Mutant D99A of Bovine Pancreatic PLA2, 1.9 A Orthorhombic Form

Enzymatic activity of Carboxylic Ester Hydrolase, Single Mutant D99A of Bovine Pancreatic PLA2, 1.9 A Orthorhombic Form

All present enzymatic activity of Carboxylic Ester Hydrolase, Single Mutant D99A of Bovine Pancreatic PLA2, 1.9 A Orthorhombic Form:
3.1.1.4;

Protein crystallography data

The structure of Carboxylic Ester Hydrolase, Single Mutant D99A of Bovine Pancreatic PLA2, 1.9 A Orthorhombic Form, PDB code: 1kvx was solved by M.Sundaralingam, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.560, 64.570, 37.990, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 31.3

Calcium Binding Sites:

The binding sites of Calcium atom in the Carboxylic Ester Hydrolase, Single Mutant D99A of Bovine Pancreatic PLA2, 1.9 A Orthorhombic Form (pdb code 1kvx). 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 D99A of Bovine Pancreatic PLA2, 1.9 A Orthorhombic Form, PDB code: 1kvx:

Calcium binding site 1 out of 1 in 1kvx

Go back to Calcium Binding Sites List in 1kvx
Calcium binding site 1 out of 1 in the Carboxylic Ester Hydrolase, Single Mutant D99A of Bovine Pancreatic PLA2, 1.9 A Orthorhombic Form


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 D99A of Bovine Pancreatic PLA2, 1.9 A Orthorhombic Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca124

b:18.9
occ:1.00
 O A:TYR28 2.1 13.2 1.0
O A:GLY32 2.2 21.4 1.0
O A:HOH226 2.2 45.9 1.0
OD2 A:ASP49 2.4 17.9 1.0
O A:HOH227 2.4 13.6 1.0
O A:GLY30 2.5 19.4 1.0
OD1 A:ASP49 2.5 9.9 1.0
CG A:ASP49 2.8 15.8 1.0
C A:TYR28 3.3 10.4 1.0
C A:GLY32 3.4 21.4 1.0
C A:GLY30 3.7 18.5 1.0
N A:GLY30 3.9 14.8 1.0
CA A:TYR28 4.0 9.9 1.0
O A:HOH261 4.1 42.8 1.0
N A:GLY32 4.1 22.3 1.0
CA A:GLY32 4.3 21.4 1.0
N A:CYS29 4.3 11.0 1.0
CB A:ASP49 4.4 13.3 1.0
N A:GLY33 4.4 18.7 1.0
C A:LEU31 4.4 21.3 1.0
CA A:GLY30 4.4 18.9 1.0
CB A:TYR28 4.4 11.5 1.0
O A:HOH228 4.5 20.9 1.0
O A:HOH259 4.5 40.0 1.0
C A:CYS29 4.5 13.5 1.0
CA A:CYS29 4.5 12.7 1.0
CA A:GLY33 4.5 15.4 1.0
N A:LEU31 4.7 21.6 1.0
O A:LEU31 4.7 21.3 1.0
O A:HOH274 4.8 36.2 1.0
O A:HOH280 4.8 39.9 1.0
CA A:LEU31 4.9 21.5 1.0
O A:HOH273 4.9 27.0 1.0

Reference:

K.Sekar, R.Biswas, Y.Li, M.Tsai, M.Sundaralingam. Structures of the Catalytic Site Mutants D99A and H48Q and the Calcium-Loop Mutant D49E of Phospholipase A2. Acta Crystallogr.,Sect.D V. 55 443 1999.
ISSN: ISSN 0907-4449
PubMed: 10089353
DOI: 10.1107/S0907444998013699
Page generated: Mon Jul 7 16:34:35 2025

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