Chlorine in PDB 7oxj: Ttslyd with M8A Pseudo-Wild-Type S2 Peptide

All present enzymatic activity of Ttslyd with M8A Pseudo-Wild-Type S2 Peptide:
5.2.1.8;

The structure of Ttslyd with M8A Pseudo-Wild-Type S2 Peptide, PDB code: 7oxj was solved by S.Pazicky, J.Lei, C.Loew, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.68 / 1.85
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	49.282, 49.282, 130.7, 90, 90, 120
R / Rfree (%)	19.8 / 22.4

The structure of Ttslyd with M8A Pseudo-Wild-Type S2 Peptide also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Nickel	(Ni)	1 atom

The binding sites of Chlorine atom in the Ttslyd with M8A Pseudo-Wild-Type S2 Peptide (pdb code 7oxj). 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 Ttslyd with M8A Pseudo-Wild-Type S2 Peptide, PDB code: 7oxj:

Chlorine binding site 1 out of 1 in the Ttslyd with M8A Pseudo-Wild-Type S2 Peptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Ttslyd with M8A Pseudo-Wild-Type S2 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl206 b:69.6 occ:1.00 N A:LEU30 3.3 46.8 1.0 N A:ALA148 3.4 68.5 1.0 CA A:HIS147 3.5 80.6 1.0 CB A:HIS147 3.6 84.8 1.0 CG A:ASN35 3.6 68.6 1.0 CA A:TYR29 3.6 48.9 1.0 ND2 A:ASN35 3.8 66.0 1.0 OD1 A:ASN35 3.9 71.8 1.0 CB A:ASN35 3.9 58.4 1.0 C A:TYR29 3.9 49.7 1.0 C A:HIS147 4.0 73.7 1.0 O A:SER151 4.0 117.1 1.0 CB A:LEU30 4.1 52.8 1.0 ND1 A:HIS147 4.1 98.8 1.0 CB A:TYR29 4.1 48.9 1.0 CA A:LEU30 4.3 49.1 1.0 CG A:HIS147 4.3 95.8 1.0 CB A:ALA148 4.3 59.1 1.0 O A:SER28 4.5 51.6 1.0 CA A:ALA148 4.5 62.9 1.0 O A:GLY146 4.6 79.1 1.0 CB A:SER151 4.7 123.0 1.0 N A:HIS147 4.8 77.7 1.0 N A:TYR29 4.8 45.2 1.0 CA A:SER151 4.8 118.7 1.0 C A:SER151 4.9 116.2 1.0 O A:LEU30 4.9 51.9 1.0

S.Pazicky, A.A.Werle, J.Lei, C.Low, U.Weininger. Impact of Distant Peptide Substrate Residues on Enzymatic Activity of Slyd. Cell.Mol.Life Sci. V. 79 138 2022.
ISSN: ESSN 1420-9071
PubMed: 35184231
DOI: 10.1007/S00018-022-04179-4