Chlorine in PDB 6cfq: Crystal Structure of the D141N Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound

Enzymatic activity of Crystal Structure of the D141N Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound

All present enzymatic activity of Crystal Structure of the D141N Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound:
1.11.1.21;

Protein crystallography data

The structure of Crystal Structure of the D141N Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound, PDB code: 6cfq was solved by P.C.Loewen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 96.32 / 1.72
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 100.641, 115.506, 174.546, 90.00, 90.00, 90.00
R / Rfree (%) 14.1 / 17

Other elements in 6cfq:

The structure of Crystal Structure of the D141N Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound also contains other interesting chemical elements:

Iron (Fe) 2 atoms
Sodium (Na) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the D141N Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound (pdb code 6cfq). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of the D141N Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound, PDB code: 6cfq:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 6cfq

Go back to Chlorine Binding Sites List in 6cfq
Chlorine binding site 1 out of 2 in the Crystal Structure of the D141N Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the D141N Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl803

b:34.3
occ:1.00
O A:HOH1495 2.9 20.1 1.0
O A:HOH1650 3.0 19.7 1.0
O A:HOH1555 3.2 22.1 1.0
N A:GLY124 3.4 16.8 1.0
CG2 A:VAL200 3.5 28.6 1.0
CG A:GLU198 3.5 46.0 1.0
CB A:GLU198 3.6 37.0 1.0
O A:HOH1524 3.7 35.9 1.0
CA A:GLY124 4.0 16.6 1.0
CB A:ARG123 4.3 17.4 1.0
C A:ARG123 4.4 16.4 1.0
CA A:ARG123 4.4 15.7 1.0
CD A:GLU198 4.5 46.9 1.0
OE1 A:GLU128 4.6 24.1 1.0
NA A:NA802 4.6 17.6 1.0
O A:GLY124 4.7 17.4 1.0
C A:GLY124 4.7 16.7 1.0
OE2 A:GLU128 4.8 28.2 1.0
O A:HOH1236 4.8 21.4 1.0
CG A:ARG123 4.8 18.3 1.0
CB A:VAL200 4.9 26.7 1.0
CD A:GLU128 4.9 26.9 1.0
OE2 A:GLU198 4.9 44.7 1.0
CG A:GLN130 4.9 17.9 1.0

Chlorine binding site 2 out of 2 in 6cfq

Go back to Chlorine Binding Sites List in 6cfq
Chlorine binding site 2 out of 2 in the Crystal Structure of the D141N Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of the D141N Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl803

b:30.2
occ:1.00
O B:HOH1628 3.1 16.7 1.0
O B:HOH1486 3.1 21.6 1.0
O B:HOH1549 3.1 20.3 1.0
N B:GLY124 3.3 16.5 1.0
CG2 B:VAL200 3.5 22.8 1.0
CG B:GLU198 3.6 36.2 1.0
CB B:GLU198 3.6 30.0 1.0
N3 B:NIZ809 3.7 28.9 0.8
N2 B:NIZ809 4.0 34.6 0.8
CA B:GLY124 4.0 15.5 1.0
CB B:ARG123 4.2 16.4 1.0
C B:ARG123 4.3 16.3 1.0
CA B:ARG123 4.3 15.1 1.0
CD B:GLU198 4.4 40.9 1.0
OE1 B:GLU128 4.4 27.2 1.0
OE2 B:GLU128 4.6 28.1 1.0
NA B:NA802 4.6 17.6 1.0
O B:GLY124 4.7 17.0 1.0
C B:GLY124 4.7 16.8 1.0
OE2 B:GLU198 4.7 38.5 1.0
O B:HOH1250 4.8 18.9 1.0
CG B:ARG123 4.8 17.4 1.0
CD B:GLU128 4.8 27.1 1.0
CG B:GLN130 4.9 17.3 1.0
CB B:VAL200 4.9 21.0 1.0

Reference:

P.C.Loewen, P.C.Loewen. N/A N/A.
Page generated: Sat Dec 12 12:49:32 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy