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Chlorine in PDB 3el6: Crystal Structure of the Erythromycin Dehydratase

Enzymatic activity of Crystal Structure of the Erythromycin Dehydratase

All present enzymatic activity of Crystal Structure of the Erythromycin Dehydratase:
4.2.1.61;

Protein crystallography data

The structure of Crystal Structure of the Erythromycin Dehydratase, PDB code: 3el6 was solved by A.T.Keatinge-Clay, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.55 / 1.85
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 66.997, 66.997, 186.238, 90.00, 90.00, 90.00
R / Rfree (%) 19.7 / 22.7

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Erythromycin Dehydratase (pdb code 3el6). 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 the Erythromycin Dehydratase, PDB code: 3el6:

Chlorine binding site 1 out of 1 in 3el6

Go back to Chlorine Binding Sites List in 3el6
Chlorine binding site 1 out of 1 in the Crystal Structure of the Erythromycin Dehydratase


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 Erythromycin Dehydratase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl290

b:29.6
occ:1.00
O A:HOH324 3.0 30.4 1.0
N A:ASP20 3.2 23.1 1.0
CG A:ARG8 3.5 31.9 1.0
NE A:ARG8 3.5 32.4 1.0
CD A:ARG8 3.7 30.7 1.0
CA A:VAL19 3.9 23.8 1.0
CB A:ASP20 3.9 24.3 1.0
OD2 A:ASP20 3.9 37.8 1.0
CG A:ASP20 3.9 30.9 1.0
C A:VAL19 4.0 22.2 1.0
O A:ALA18 4.1 24.5 1.0
CA A:ASP20 4.2 23.9 1.0
N A:ARG8 4.4 27.6 1.0
CG1 A:VAL19 4.5 27.8 1.0
CB A:ARG8 4.6 29.1 1.0
OD1 A:ASP20 4.6 33.7 1.0
CZ A:ARG8 4.7 31.6 1.0
N A:VAL19 4.7 23.0 1.0
C A:ALA18 4.8 23.9 1.0
CB A:VAL19 4.8 23.6 1.0
O A:ASP20 4.9 24.8 1.0
O A:GLY6 4.9 33.5 1.0
C A:VAL7 4.9 28.8 1.0
CA A:VAL7 5.0 29.6 1.0

Reference:

A.Keatinge-Clay, A.T.Keatinge-Clay. N/A N/A.
ISSN: ISSN 0022-2836
PubMed: 18952099
DOI: 10.1016/J.JMB.2008.09.084
Page generated: Fri Jul 11 04:49:16 2025

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