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Chlorine in PDB 3jzf: Crystal Structure of Biotin Carboxylase From E. Coli in Complex with Benzimidazoles Series

Enzymatic activity of Crystal Structure of Biotin Carboxylase From E. Coli in Complex with Benzimidazoles Series

All present enzymatic activity of Crystal Structure of Biotin Carboxylase From E. Coli in Complex with Benzimidazoles Series:
6.3.4.14; 6.4.1.2;

Protein crystallography data

The structure of Crystal Structure of Biotin Carboxylase From E. Coli in Complex with Benzimidazoles Series, PDB code: 3jzf was solved by P.Orth, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.94 / 2.13
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 84.370, 107.514, 122.345, 90.00, 90.00, 90.00
R / Rfree (%) 20.3 / 23.6

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Biotin Carboxylase From E. Coli in Complex with Benzimidazoles Series (pdb code 3jzf). 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 Crystal Structure of Biotin Carboxylase From E. Coli in Complex with Benzimidazoles Series, PDB code: 3jzf:

Chlorine binding site 1 out of 1 in 3jzf

Go back to Chlorine Binding Sites List in 3jzf
Chlorine binding site 1 out of 1 in the Crystal Structure of Biotin Carboxylase From E. Coli in Complex with Benzimidazoles Series


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 Biotin Carboxylase From E. Coli in Complex with Benzimidazoles Series within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl466

b:42.0
occ:1.00
 CL25 B:JZK466 0.0 42.0 1.0
C24 B:JZK466 1.7 39.1 1.0
C19 B:JZK466 2.7 40.2 1.0
C23 B:JZK466 2.7 35.8 1.0
C18 B:JZK466 2.9 43.0 1.0
O B:ILE287 3.3 27.3 1.0
OH B:TYR199 3.3 24.5 1.0
O B:HOH614 3.4 30.5 1.0
CD B:LYS116 3.5 32.2 1.0
CG B:LYS116 3.6 28.0 1.0
CB B:GLU288 3.7 23.8 1.0
NZ B:LYS159 3.9 32.8 1.0
C20 B:JZK466 4.0 37.2 1.0
C22 B:JZK466 4.0 35.8 1.0
CD B:GLU288 4.1 42.3 1.0
CB B:LYS116 4.1 24.7 1.0
C B:ILE287 4.1 26.7 1.0
CE B:LYS159 4.1 34.1 1.0
OE1 B:GLU288 4.2 34.3 1.0
CG B:GLU288 4.2 29.2 1.0
N17 B:JZK466 4.3 44.8 1.0
O B:HOH603 4.3 27.0 1.0
CA B:GLY164 4.5 32.0 1.0
OE2 B:GLU288 4.5 38.1 1.0
CE B:LYS116 4.5 42.0 1.0
C21 B:JZK466 4.5 37.4 1.0
N26 B:JZK466 4.6 47.1 1.0
CZ B:TYR199 4.7 27.5 1.0
CA B:GLU288 4.7 22.2 1.0
N B:GLU288 4.7 22.0 1.0
C16 B:JZK466 4.8 45.7 1.0
CB B:ILE287 4.9 27.9 1.0
CA B:ILE287 5.0 23.8 1.0

Reference:

C.C.Cheng, G.W.Shipps, Z.Yang, B.Sun, N.Kawahata, K.A.Soucy, A.Soriano, P.Orth, L.Xiao, P.Mann, T.Black. Discovery and Optimization of Antibacterial Accc Inhibitors. Bioorg.Med.Chem.Lett. V. 19 6507 2009.
ISSN: ISSN 0960-894X
PubMed: 19875284
DOI: 10.1016/J.BMCL.2009.10.057
Page generated: Sat Jul 20 22:18:02 2024

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