Chlorine in PDB 2zp3: Carboxylic Ester Hydrolase, Single Mutant D49N of Bovine Pancreatic PLA2 Enzyme

Enzymatic activity of Carboxylic Ester Hydrolase, Single Mutant D49N of Bovine Pancreatic PLA2 Enzyme

All present enzymatic activity of Carboxylic Ester Hydrolase, Single Mutant D49N of Bovine Pancreatic PLA2 Enzyme:
3.1.1.4;

Protein crystallography data

The structure of Carboxylic Ester Hydrolase, Single Mutant D49N of Bovine Pancreatic PLA2 Enzyme, PDB code: 2zp3 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)*	22.89 / 1.90
*Space group*	P 3₁ 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	45.786, 45.786, 101.943, 90.00, 90.00, 120.00
*R / R_free (%)*	19.1 / 23.8

Other elements in 2zp3:

The structure of Carboxylic Ester Hydrolase, Single Mutant D49N of Bovine Pancreatic PLA2 Enzyme also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Carboxylic Ester Hydrolase, Single Mutant D49N of Bovine Pancreatic PLA2 Enzyme (pdb code 2zp3). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Carboxylic Ester Hydrolase, Single Mutant D49N of Bovine Pancreatic PLA2 Enzyme, PDB code: 2zp3:

Chlorine binding site 1 out of 1 in 2zp3

Go back to

Chlorine Binding Sites List in 2zp3

Chlorine binding site 1 out of 1 in the Carboxylic Ester Hydrolase, Single Mutant D49N of Bovine Pancreatic PLA2 Enzyme

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Carboxylic Ester Hydrolase, Single Mutant D49N of Bovine Pancreatic PLA2 Enzyme within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl125 b:19.1 occ:1.00	CE	A:LYS12	3.0	22.3	1.0
	NZ	A:LYS12	3.1	17.6	1.0
	N	A:ILE82	3.2	14.3	1.0
	NH2	A:ARG100	3.6	21.0	1.0
	CA	A:GLU81	3.8	15.0	1.0
	CD1	A:ILE104	3.8	10.7	1.0
	C	A:GLU81	4.0	13.8	1.0
	O	A:ILE82	4.0	13.2	1.0
	NE	A:ARG100	4.0	16.5	1.0
	CB	A:ILE82	4.1	11.4	1.0
	CA	A:ILE82	4.1	12.2	1.0
	CG1	A:ILE104	4.1	10.2	1.0
	CZ	A:ARG100	4.1	19.9	1.0
	CB	A:GLU81	4.3	18.1	1.0
	CG1	A:ILE82	4.4	12.0	1.0
	CD	A:LYS12	4.4	19.3	1.0
	C	A:ILE82	4.5	13.2	1.0
	O	A:ASN80	4.5	16.8	1.0
	O	A:HOH330	4.8	31.6	1.0
	CG	A:GLU81	4.9	24.1	1.0
	CD1	A:ILE82	4.9	11.9	1.0
	N	A:GLU81	5.0	14.2	1.0
	O	A:HOH236	5.0	33.0	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: Fri Jul 11 02:55:47 2025

Last articles

Fe in 2YXO
Fe in 2YRS
Fe in 2YXC
Fe in 2YNM
Fe in 2YVJ
Fe in 2YP1
Fe in 2YU2
Fe in 2YU1
Fe in 2YQB
Fe in 2YOO

	© Copyright 2008-2020 by atomistry.com
Home \| Site Map \| Copyright \| Contact us \| Privacy