Chlorine in PDB 5ckv: Dahp Synthase From Mycobacterium Tuberculosis, Fully Inhibited By Tyrosine, Phenylalanine, and Tryptophan

All present enzymatic activity of Dahp Synthase From Mycobacterium Tuberculosis, Fully Inhibited By Tyrosine, Phenylalanine, and Tryptophan:
2.5.1.54;

The structure of Dahp Synthase From Mycobacterium Tuberculosis, Fully Inhibited By Tyrosine, Phenylalanine, and Tryptophan, PDB code: 5ckv was solved by S.Munack, U.Krengel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.30 / 2.79
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	204.760, 204.760, 66.774, 90.00, 90.00, 120.00
R / Rfree (%)	17.5 / 22.6

The structure of Dahp Synthase From Mycobacterium Tuberculosis, Fully Inhibited By Tyrosine, Phenylalanine, and Tryptophan also contains other interesting chemical elements:

Manganese

(Mn)

2 atoms

The binding sites of Chlorine atom in the Dahp Synthase From Mycobacterium Tuberculosis, Fully Inhibited By Tyrosine, Phenylalanine, and Tryptophan (pdb code 5ckv). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Dahp Synthase From Mycobacterium Tuberculosis, Fully Inhibited By Tyrosine, Phenylalanine, and Tryptophan, PDB code: 5ckv:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Dahp Synthase From Mycobacterium Tuberculosis, Fully Inhibited By Tyrosine, Phenylalanine, and Tryptophan


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Dahp Synthase From Mycobacterium Tuberculosis, Fully Inhibited By Tyrosine, Phenylalanine, and Tryptophan within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl501 b:67.9 occ:1.00 H A:ALA141 2.7 63.9 1.0 HB2 A:ASP140 2.9 63.6 1.0 HB2 A:ALA141 3.3 54.0 1.0 HH12 A:ARG135 3.5 0.7 1.0 N A:ALA141 3.5 53.3 1.0 HA A:ASP140 3.6 60.2 1.0 HB3 A:ALA141 3.7 54.0 1.0 CB A:ASP140 3.8 53.0 1.0 CB A:ALA141 3.9 45.0 1.0 HH11 A:ARG135 4.0 0.7 1.0 NH1 A:ARG135 4.0 83.9 1.0 CA A:ASP140 4.1 50.2 1.0 HB3 A:ASP140 4.1 63.6 1.0 C A:ASP140 4.3 51.0 1.0 CA A:ALA141 4.3 44.9 1.0 HA A:ALA141 4.7 53.9 1.0 HB1 A:ALA141 4.8 54.0 1.0 CG A:ASP140 4.9 64.3 1.0

Chlorine binding site 2 out of 2 in the Dahp Synthase From Mycobacterium Tuberculosis, Fully Inhibited By Tyrosine, Phenylalanine, and Tryptophan


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Dahp Synthase From Mycobacterium Tuberculosis, Fully Inhibited By Tyrosine, Phenylalanine, and Tryptophan within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl501 b:54.9 occ:1.00 HH21 B:ARG23 2.3 45.6 1.0 H B:LEU18 2.6 52.0 1.0 HD2 B:ARG23 3.0 61.4 1.0 NH2 B:ARG23 3.1 38.0 1.0 HA B:PRO17 3.1 69.2 1.0 HH22 B:ARG23 3.3 45.6 1.0 HB2 B:LEU18 3.4 45.8 1.0 N B:LEU18 3.4 43.3 1.0 O B:HOH609 3.6 41.8 1.0 HD1 B:TYR508 3.6 52.4 1.0 HD3 B:ARG23 3.6 61.4 1.0 HG B:LEU18 3.6 39.9 1.0 CD B:ARG23 3.8 51.2 1.0 HE1 B:TYR508 3.8 44.2 1.0 CA B:PRO17 3.9 57.7 1.0 CB B:LEU18 4.1 38.1 1.0 HD12 B:LEU18 4.2 39.4 1.0 CZ B:ARG23 4.2 49.5 1.0 C B:PRO17 4.2 55.5 1.0 CD1 B:TYR508 4.2 43.7 1.0 CG B:LEU18 4.3 33.3 1.0 CE1 B:TYR508 4.3 36.8 1.0 CA B:LEU18 4.4 41.4 1.0 HB3 B:PRO17 4.4 62.6 1.0 HB2 B:PRO17 4.4 62.6 1.0 NE B:ARG23 4.4 53.1 1.0 HB2 B:ARG23 4.4 55.0 1.0 CB B:PRO17 4.5 52.2 1.0 CD1 B:LEU18 4.8 32.8 1.0 O B:PRO16 4.9 72.0 1.0 HB3 B:LEU18 4.9 45.8 1.0 CG B:ARG23 4.9 42.3 1.0

S.Munack, K.Roderer, M.Okvist, J.Kamarauskaite, S.Sasso, A.Van Eerde, P.Kast, U.Krengel. Remote Control By Inter-Enzyme Allostery: A Novel Paradigm For Regulation of the Shikimate Pathway. J.Mol.Biol. V. 428 1237 2016.
ISSN: ESSN 1089-8638
PubMed: 26776476
DOI: 10.1016/J.JMB.2016.01.001