Chlorine in PDB 4rqo: Crystal Structure of L-Serine Dehydratase From Legionella Pneumophila

All present enzymatic activity of Crystal Structure of L-Serine Dehydratase From Legionella Pneumophila:
4.3.1.17;

The structure of Crystal Structure of L-Serine Dehydratase From Legionella Pneumophila, PDB code: 4rqo was solved by J.B.Thoden, H.M.Holden, G.A.Grant, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.45 / 2.25
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	81.390, 81.390, 267.521, 90.00, 90.00, 120.00
R / Rfree (%)	19.8 / 25.8

The structure of Crystal Structure of L-Serine Dehydratase From Legionella Pneumophila also contains other interesting chemical elements:

Iron

(Fe)

8 atoms

The binding sites of Chlorine atom in the Crystal Structure of L-Serine Dehydratase From Legionella Pneumophila (pdb code 4rqo). 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 L-Serine Dehydratase From Legionella Pneumophila, PDB code: 4rqo:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of L-Serine Dehydratase From Legionella Pneumophila


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 L-Serine Dehydratase From Legionella Pneumophila within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl502 b:69.6 occ:1.00 OG B:SER10 3.9 36.5 1.0 CB B:SER10 4.3 36.5 1.0 O B:HOH668 4.4 33.5 1.0 CE1 B:PHE152 4.4 46.9 1.0 O B:GLY150 4.4 32.6 1.0 CZ B:PHE152 4.5 45.7 1.0 O B:GLY151 4.5 26.8 1.0 CD1 B:LEU25 4.6 30.8 1.0 C B:GLY151 4.7 26.1 1.0 CD1 B:PHE152 4.7 46.1 1.0 CE2 B:PHE152 4.8 41.5 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of L-Serine Dehydratase From Legionella Pneumophila


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 L-Serine Dehydratase From Legionella Pneumophila within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl503 b:60.9 occ:1.00 CB B:LYS118 3.7 37.5 1.0 CD B:LYS118 3.8 58.2 1.0 N B:LYS118 3.9 34.5 1.0 CG B:LYS118 4.1 45.6 1.0 CA B:LEU116 4.1 29.4 1.0 OE2 B:GLU119 4.2 50.0 1.0 CA B:LYS118 4.2 38.7 1.0 O B:HOH672 4.3 51.1 1.0 N B:GLN117 4.3 26.5 1.0 C B:LEU116 4.4 27.6 1.0 CD2 B:LEU116 4.4 38.1 1.0 CG B:GLU119 4.4 39.0 1.0 C B:LYS118 4.5 35.3 1.0 CB B:LEU116 4.6 31.4 1.0 CD B:GLU119 4.7 42.2 1.0 O B:PHE115 4.8 30.6 1.0 N B:GLU119 4.9 35.0 1.0 O B:LYS118 4.9 36.6 1.0 C B:GLN117 5.0 32.6 1.0 CE B:LYS118 5.0 69.0 1.0

J.B.Thoden, H.M.Holden, G.A.Grant. Structure of L-Serine Dehydratase From Legionella Pneumophila: Novel Use of the C-Terminal Cysteine As An Intrinsic Competitive Inhibitor. Biochemistry 2014.
ISSN: ISSN 0006-2960
PubMed: 25380533
DOI: 10.1021/BI501253W