Chlorine in PDB 7oxg: Ttslyd Fkbp Domain with M8A Pseudo-Wild-Type S2 Peptide

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

The structure of Ttslyd Fkbp Domain with M8A Pseudo-Wild-Type S2 Peptide, PDB code: 7oxg 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)	39.59 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	34.681, 82.525, 42.268, 90, 110.52, 90
R / Rfree (%)	20.2 / 24.7

The binding sites of Chlorine atom in the Ttslyd Fkbp Domain with M8A Pseudo-Wild-Type S2 Peptide (pdb code 7oxg). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Ttslyd Fkbp Domain with M8A Pseudo-Wild-Type S2 Peptide, PDB code: 7oxg:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Ttslyd Fkbp Domain 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 Fkbp Domain with M8A Pseudo-Wild-Type S2 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:21.6 occ:1.00 O A:HOH316 2.6 36.3 0.5 N A:LEU30 3.2 22.4 1.0 ND2 A:ASN35 3.3 19.8 1.0 N A:ALA100 3.4 22.2 1.0 CA A:HIS99 3.5 26.5 1.0 ND1 A:HIS99 3.5 21.3 1.0 CA A:TYR29 3.6 16.4 1.0 CG A:ASN35 3.6 30.7 1.0 CB A:HIS99 3.7 21.5 1.0 CB A:ASN35 3.8 20.1 1.0 CB A:TYR29 3.9 17.0 1.0 C A:TYR29 3.9 23.5 1.0 O A:HOH315 3.9 69.4 1.0 C A:HIS99 4.0 30.4 1.0 CG A:HIS99 4.1 27.0 1.0 CB A:LEU30 4.2 18.7 1.0 CA A:LEU30 4.2 21.2 1.0 OD1 A:ASN35 4.3 23.6 1.0 O A:GLY98 4.4 23.2 1.0 CB A:ALA100 4.5 24.6 1.0 CA A:ALA100 4.5 25.9 1.0 O A:LEU30 4.5 24.1 1.0 O A:SER28 4.5 17.9 1.0 CE1 C:PHE11 4.6 19.9 1.0 CE1 A:HIS99 4.7 23.2 1.0 N A:HIS99 4.7 24.7 1.0 N A:TYR29 4.8 19.1 1.0 C A:LEU30 4.9 19.6 1.0 O A:ALA100 5.0 27.9 1.0

Chlorine binding site 2 out of 2 in the Ttslyd Fkbp Domain 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 2 of Ttslyd Fkbp Domain with M8A Pseudo-Wild-Type S2 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl201 b:27.6 occ:1.00 O B:HOH307 3.1 24.6 1.0 N B:LEU30 3.2 30.3 1.0 ND2 B:ASN35 3.3 31.4 1.0 N B:ALA100 3.4 35.8 1.0 ND1 B:HIS99 3.4 48.5 1.0 CA B:TYR29 3.5 27.9 1.0 CG B:ASN35 3.6 37.7 1.0 CA B:HIS99 3.7 38.2 1.0 CB B:ASN35 3.7 41.2 1.0 CB B:TYR29 3.8 31.3 1.0 C B:TYR29 3.8 31.5 1.0 CB B:HIS99 3.9 39.4 1.0 C B:HIS99 4.1 46.6 1.0 CG B:HIS99 4.1 46.8 1.0 CB B:LEU30 4.1 28.3 1.0 CA B:LEU30 4.2 28.9 1.0 OD1 B:ASN35 4.3 37.2 1.0 CB B:ALA100 4.3 41.0 1.0 CA B:ALA100 4.4 42.2 1.0 O B:GLY98 4.5 50.2 1.0 O B:SER28 4.5 27.4 1.0 CE1 B:HIS99 4.6 50.0 1.0 O B:LEU30 4.6 26.2 1.0 N B:TYR29 4.7 27.6 1.0 CE1 D:PHE11 4.8 34.0 1.0 N B:HIS99 4.9 40.2 1.0 C B:LEU30 4.9 34.4 1.0 O B:ALA100 4.9 44.4 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