Chlorine in PDB 7mde: Full-Length S95A Clbp

All present enzymatic activity of Full-Length S95A Clbp:
3.5.2.6;

The structure of Full-Length S95A Clbp, PDB code: 7mde was solved by J.A.Velilla, M.R.Volpe, R.Gaudet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.74 / 2.70
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	97.475, 97.475, 183.973, 90, 90, 90
R / Rfree (%)	19.5 / 23.5

The binding sites of Chlorine atom in the Full-Length S95A Clbp (pdb code 7mde). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Full-Length S95A Clbp, PDB code: 7mde:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Full-Length S95A Clbp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Full-Length S95A Clbp within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl610 b:78.0 occ:1.00 O A:HOH712 2.9 62.3 1.0 NZ A:LYS204 3.1 71.6 1.0 NH2 A:ARG213 3.2 97.1 1.0 NH1 A:ARG113 3.2 82.3 1.0 NH1 A:ARG213 3.7 81.7 1.0 CZ A:ARG213 3.8 88.8 1.0 O A:HOH755 4.0 82.5 1.0 NH2 A:ARG113 4.2 83.4 1.0 CZ A:ARG113 4.2 86.3 1.0 CD A:LYS204 4.2 63.4 1.0 CE A:LYS204 4.2 68.9 1.0 CG2 A:THR202 4.6 54.1 1.0 CB A:THR202 4.6 53.5 1.0 NE A:ARG213 5.0 77.4 1.0

Chlorine binding site 2 out of 3 in the Full-Length S95A Clbp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Full-Length S95A Clbp within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl611 b:80.6 occ:1.00 O A:HOH784 3.2 68.7 1.0 NH2 A:ARG255 3.4 68.3 1.0 NZ A:LYS227 3.9 91.9 1.0 CD A:LYS227 3.9 71.8 1.0 CE A:LYS227 4.6 83.1 1.0 CZ A:ARG255 4.7 68.9 1.0 CG2 A:THR205 4.8 49.1 1.0

Chlorine binding site 3 out of 3 in the Full-Length S95A Clbp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Full-Length S95A Clbp within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl612 b:55.2 occ:1.00 O A:ILE309 3.5 50.1 1.0 OD1 A:ASN307 4.0 40.4 1.0 CE2 A:PHE316 4.1 46.3 1.0 CD2 A:PHE316 4.1 40.9 1.0 ND2 A:ASN307 4.1 39.0 1.0 CE2 A:PHE184 4.2 40.0 1.0 CB A:ILE309 4.3 48.7 1.0 C A:ILE309 4.3 49.1 1.0 CG A:ASN307 4.3 40.9 1.0 O A:HOH787 4.4 44.9 1.0 CG2 A:ILE309 4.4 36.6 1.0 CD2 A:PHE184 4.5 40.8 1.0 CZ A:PHE184 4.6 40.6 1.0 CA A:ILE309 4.8 52.1 1.0

J.A.Velilla, M.R.Volpe, G.E.Kenney, R.M.Walsh Jr., E.P.Balskus, R.Gaudet. Structural Basis of Colibactin Activation By the Clbp Peptidase. Nat.Chem.Biol. 2022.
ISSN: ESSN 1552-4469
PubMed: 36253550
DOI: 10.1038/S41589-022-01142-Z