Chlorine in PDB 4d7n: Tetr(D) in Complex with Anhydrotetracycline and Potassium

The structure of Tetr(D) in Complex with Anhydrotetracycline and Potassium, PDB code: 4d7n was solved by S.Werten, D.Dalm, G.J.Palm, W.Hinrichs, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	63.62 / 1.76
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	68.065, 68.065, 178.909, 90.00, 90.00, 90.00
R / Rfree (%)	18.943 / 22.507

The structure of Tetr(D) in Complex with Anhydrotetracycline and Potassium also contains other interesting chemical elements:

Potassium

(K)

2 atoms

The binding sites of Chlorine atom in the Tetr(D) in Complex with Anhydrotetracycline and Potassium (pdb code 4d7n). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Tetr(D) in Complex with Anhydrotetracycline and Potassium, PDB code: 4d7n:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Tetr(D) in Complex with Anhydrotetracycline and Potassium


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Tetr(D) in Complex with Anhydrotetracycline and Potassium within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl302 b:29.0 occ:1.00 OG A:SER74 3.1 24.7 1.0 N A:SER74 3.3 25.0 1.0 CB A:SER77 3.6 24.4 1.0 CB A:SER74 3.6 24.7 1.0 OG A:SER77 4.0 23.8 1.0 CA A:SER74 4.0 23.9 1.0 CG A:GLU73 4.1 25.9 1.0 CA A:GLU73 4.1 26.6 1.0 C A:GLU73 4.2 26.1 1.0 O A:HOH2076 4.4 59.2 1.0 CB A:GLU73 4.6 25.6 1.0 O A:GLY72 4.7 30.7 1.0 O A:HOH2077 4.8 47.7 1.0 O A:HOH2075 4.9 49.2 1.0 O A:SER74 5.0 22.8 1.0 CA A:SER77 5.0 22.3 1.0

Chlorine binding site 2 out of 4 in the Tetr(D) in Complex with Anhydrotetracycline and Potassium


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Tetr(D) in Complex with Anhydrotetracycline and Potassium within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl303 b:29.2 occ:1.00 N A:LEU4 3.1 26.7 1.0 O A:HOH2007 3.4 42.1 1.0 CB A:LEU4 3.8 24.5 1.0 CA A:LEU4 3.8 25.5 1.0 CD A:ARG3 3.9 37.5 1.0 NE A:ARG3 3.9 37.3 1.0 C A:ARG3 4.1 29.3 1.0 CA A:ARG3 4.1 32.8 1.0 C A:LEU4 4.2 30.7 1.0 CG A:LEU4 4.3 24.4 1.0 CG A:ARG3 4.4 35.1 1.0 N A:ASN5 4.5 27.1 1.0 O A:SER2 4.6 29.1 1.0 O A:LEU4 4.7 35.6 1.0 CB A:ARG3 4.9 35.0 1.0 CD1 A:LEU4 5.0 26.3 1.0

Chlorine binding site 3 out of 4 in the Tetr(D) in Complex with Anhydrotetracycline and Potassium


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Tetr(D) in Complex with Anhydrotetracycline and Potassium within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl304 b:36.6 occ:1.00 O A:HOH2014 3.0 44.1 1.0 N A:GLU7 3.3 28.3 1.0 O A:HOH2011 3.4 49.9 1.0 N A:ARG6 3.6 28.2 0.5 N A:ARG6 3.6 27.9 0.5 ND2 A:ASN5 3.7 38.3 1.0 CB A:ASN5 3.7 30.1 1.0 CB A:ARG6 3.8 30.2 0.5 CG A:ASN5 3.8 35.4 1.0 CB A:ARG6 3.8 29.1 0.5 CB A:GLU7 3.8 34.5 1.0 CA A:ARG6 4.0 27.7 0.5 CA A:ARG6 4.0 27.1 0.5 C A:ARG6 4.1 27.0 0.5 C A:ARG6 4.1 26.8 0.5 CA A:GLU7 4.1 30.6 1.0 C A:ASN5 4.3 27.8 1.0 O A:HOH2012 4.4 49.0 1.0 OD1 A:ASN5 4.5 33.5 1.0 CA A:ASN5 4.6 28.8 1.0 CG A:ARG6 4.9 30.0 0.5

Chlorine binding site 4 out of 4 in the Tetr(D) in Complex with Anhydrotetracycline and Potassium


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Tetr(D) in Complex with Anhydrotetracycline and Potassium within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl305 b:52.3 occ:1.00 NE1 A:TRP75 3.1 22.1 1.0 O A:HOH2109 3.4 45.1 1.0 NE2 A:GLN76 3.6 26.9 1.0 O A:HOH2081 3.8 34.6 1.0 CD2 A:LEU201 3.8 32.0 1.0 CE2 A:TRP75 4.0 21.1 1.0 CD1 A:TRP75 4.1 23.4 1.0 CZ2 A:TRP75 4.2 23.4 1.0 CG2 A:THR202 4.3 37.7 1.0 CD A:GLN76 4.4 23.5 1.0 OE1 A:GLN76 4.5 23.9 1.0 CG A:GLU198 4.5 30.4 1.0 CG A:LEU201 4.9 31.6 1.0 O A:HOH2110 4.9 53.7 1.0

S.Werten, D.Dalm, G.J.Palm, C.C.Grimm, W.Hinrichs. Tetracycline Repressor Allostery Does Not Depend on Divalent Metal Recognition. Biochemistry 2014.
ISSN: ESSN 1520-4995
PubMed: 25432019
DOI: 10.1021/BI5012805