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Chlorine in PDB 7pjc: The Structure of Candida Albicans Phosphoglucomutase with Isothiazolone Modification on CYS359

Enzymatic activity of The Structure of Candida Albicans Phosphoglucomutase with Isothiazolone Modification on CYS359

All present enzymatic activity of The Structure of Candida Albicans Phosphoglucomutase with Isothiazolone Modification on CYS359:
5.4.2.2;

Protein crystallography data

The structure of The Structure of Candida Albicans Phosphoglucomutase with Isothiazolone Modification on CYS359, PDB code: 7pjc was solved by K.Yan, D.M.F.Van Aalten, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 67.97 / 2.11
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 66.744, 86.444, 110.154, 90, 92.74, 90
R / Rfree (%) 18.9 / 25.5

Other elements in 7pjc:

The structure of The Structure of Candida Albicans Phosphoglucomutase with Isothiazolone Modification on CYS359 also contains other interesting chemical elements:

Fluorine (F) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the The Structure of Candida Albicans Phosphoglucomutase with Isothiazolone Modification on CYS359 (pdb code 7pjc). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the The Structure of Candida Albicans Phosphoglucomutase with Isothiazolone Modification on CYS359, PDB code: 7pjc:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 7pjc

Go back to Chlorine Binding Sites List in 7pjc
Chlorine binding site 1 out of 2 in the The Structure of Candida Albicans Phosphoglucomutase with Isothiazolone Modification on CYS359


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The Structure of Candida Albicans Phosphoglucomutase with Isothiazolone Modification on CYS359 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl601

b:30.3
occ:1.00
CL1 B:A4W601 0.0 30.3 1.0
C13 B:A4W601 1.8 24.4 1.0
C12 B:A4W601 2.7 23.2 1.0
C02 B:A4W601 2.8 20.5 1.0
F01 B:A4W601 3.0 28.7 1.0
CE2 B:PHE358 3.7 18.6 1.0
CD2 B:PHE358 3.7 18.6 1.0
SG B:CYS370 3.8 18.0 1.0
CD B:LYS385 3.8 22.0 1.0
CG B:LYS385 3.8 18.6 1.0
C11 B:A4W601 4.1 22.8 1.0
C03 B:A4W601 4.1 24.3 1.0
CA B:GLY371 4.2 12.1 1.0
N B:GLY371 4.3 13.9 1.0
O B:CYS370 4.3 13.7 1.0
C B:CYS370 4.4 15.2 1.0
CZ B:PHE358 4.5 14.9 1.0
CG B:PHE358 4.5 15.6 1.0
C10 B:A4W601 4.6 24.3 1.0
O B:GLY376 4.6 15.8 1.0
C B:GLY371 4.7 14.4 1.0
CB B:CYS370 4.7 13.6 1.0
N B:GLY378 4.7 13.9 1.0
CD B:GLU372 4.8 40.6 1.0
C B:GLY376 4.8 12.8 1.0
N B:GLU372 4.8 16.9 1.0
OE2 B:GLU372 4.8 37.7 1.0
N B:THR377 4.9 12.3 1.0
C B:THR377 4.9 15.6 1.0
CA B:THR377 4.9 13.6 1.0
OE1 B:GLU372 5.0 35.7 1.0

Chlorine binding site 2 out of 2 in 7pjc

Go back to Chlorine Binding Sites List in 7pjc
Chlorine binding site 2 out of 2 in the The Structure of Candida Albicans Phosphoglucomutase with Isothiazolone Modification on CYS359


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of The Structure of Candida Albicans Phosphoglucomutase with Isothiazolone Modification on CYS359 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl602

b:36.5
occ:1.00
CL1 A:A4W602 0.0 36.5 1.0
C13 A:A4W602 1.8 24.1 1.0
C02 A:A4W602 2.7 22.8 1.0
C12 A:A4W602 2.7 24.3 1.0
F01 A:A4W602 2.9 25.8 1.0
SG A:CYS370 3.5 24.3 1.0
CE2 A:PHE358 3.8 22.9 1.0
CD2 A:PHE358 3.8 24.7 1.0
CD A:LYS385 3.9 25.9 1.0
CG A:LYS385 3.9 22.2 1.0
C11 A:A4W602 4.0 27.2 1.0
CA A:GLY371 4.0 13.7 1.0
C03 A:A4W602 4.1 25.8 1.0
N A:GLY371 4.2 13.7 1.0
O A:CYS370 4.2 14.8 1.0
C A:CYS370 4.3 18.7 1.0
CZ A:PHE358 4.4 19.8 1.0
CG A:PHE358 4.5 26.1 1.0
O A:GLY376 4.6 18.8 1.0
C10 A:A4W602 4.6 27.8 1.0
CB A:CYS370 4.6 18.3 1.0
C A:GLY371 4.6 16.4 1.0
N A:GLY378 4.7 19.9 1.0
OE1 A:GLU372 4.7 36.7 1.0
C A:GLY376 4.8 20.0 1.0
C A:THR377 4.9 19.3 1.0
CA A:THR377 5.0 19.0 1.0
N A:GLU372 5.0 17.1 1.0

Reference:

K.Yan, M.Stanley, B.Kowalski, O.G.Raimi, A.T.Ferenbach, P.Wei, H.Yuan, W.Fang, D.M.F.Van Aalten. Targeting An Essential Step in the Biosynthetic Pathway of Uridine Diphosphate Glucose in Aspergillus Fumigatus To Be Published.
Page generated: Sun Jul 13 05:40:35 2025

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