Chlorine in PDB 5d8g: A Structural View on the Dissociation of E. Coli Tryptophanase

All present enzymatic activity of A Structural View on the Dissociation of E. Coli Tryptophanase:
4.1.99.1;

The structure of A Structural View on the Dissociation of E. Coli Tryptophanase, PDB code: 5d8g was solved by O.Almog, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.20 / 1.89
Space group	F 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	118.287, 120.267, 171.709, 90.00, 90.00, 90.00
R / Rfree (%)	17.4 / 21.4

The structure of A Structural View on the Dissociation of E. Coli Tryptophanase also contains other interesting chemical elements:

Magnesium	(Mg)	3 atoms
Calcium	(Ca)	1 atom
Sodium	(Na)	1 atom

The binding sites of Chlorine atom in the A Structural View on the Dissociation of E. Coli Tryptophanase (pdb code 5d8g). 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 A Structural View on the Dissociation of E. Coli Tryptophanase, PDB code: 5d8g:

Chlorine binding site 1 out of 1 in the A Structural View on the Dissociation of E. Coli Tryptophanase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of A Structural View on the Dissociation of E. Coli Tryptophanase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1001 b:13.8 occ:0.50 O A:HOH1208 3.1 11.8 1.0 NE A:ARG69 3.1 12.1 1.0 CB A:ALA65 3.7 11.1 1.0 CD A:ARG69 3.8 13.0 1.0 O A:HOH1472 4.1 41.9 1.0 CZ A:ARG69 4.1 16.2 1.0 NH2 A:ARG69 4.2 15.2 1.0 C A:ALA65 4.3 12.0 1.0 O A:ALA65 4.4 11.7 1.0 CG A:ARG69 4.5 12.6 1.0 N A:ALA66 4.5 11.8 1.0 CA A:ALA65 4.7 12.9 1.0 O A:HOH1468 4.8 20.1 1.0 CA A:ALA66 4.9 11.1 1.0

K.Green, N.Qasim, G.Gdaelvsky, A.Kogan, Y.Goldgur, A.H.Parola, O.Lotan, O.Almog. A Structural View of the Dissociation of Escherichia Coli Tryptophanase. Acta Crystallogr.,Sect.D V. 71 2364 2015.
ISSN: ESSN 1399-0047
PubMed: 26627645
DOI: 10.1107/S139900471501799X