Chlorine in PDB 5mt8: Structure of E.Coli Glpg in Complex with Peptide Derived Inhibitor Ac- Rvrha-Cmk

All present enzymatic activity of Structure of E.Coli Glpg in Complex with Peptide Derived Inhibitor Ac- Rvrha-Cmk:
3.4.21.105;

The structure of Structure of E.Coli Glpg in Complex with Peptide Derived Inhibitor Ac- Rvrha-Cmk, PDB code: 5mt8 was solved by K.R.Vinothkumar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.90 / 1.95
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	111.159, 111.159, 124.553, 90.00, 90.00, 120.00
R / Rfree (%)	20 / 22.5

The binding sites of Chlorine atom in the Structure of E.Coli Glpg in Complex with Peptide Derived Inhibitor Ac- Rvrha-Cmk (pdb code 5mt8). 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 Structure of E.Coli Glpg in Complex with Peptide Derived Inhibitor Ac- Rvrha-Cmk, PDB code: 5mt8:

Chlorine binding site 1 out of 1 in the Structure of E.Coli Glpg in Complex with Peptide Derived Inhibitor Ac- Rvrha-Cmk


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of E.Coli Glpg in Complex with Peptide Derived Inhibitor Ac- Rvrha-Cmk within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl306 b:63.9 occ:1.00 NE1 A:TRP159 3.1 55.9 1.0 N A:ALA93 3.2 75.4 1.0 CA A:ARG92 3.7 82.5 1.0 CB A:ARG92 3.7 86.1 1.0 CB A:ALA93 3.9 69.0 1.0 C A:ARG92 4.0 82.7 1.0 CE2 A:TRP159 4.0 60.4 1.0 CZ2 A:TRP159 4.1 71.6 1.0 CD1 A:TRP159 4.2 54.6 1.0 CA A:ALA93 4.2 65.5 1.0

A.Ticha, S.Stanchev, K.R.Vinothkumar, D.C.Mikles, P.Pachl, J.Began, J.Skerle, K.Svehlova, M.T.N.Nguyen, S.H.L.Verhelst, D.C.Johnson, D.A.Bachovchin, M.Lepsik, P.Majer, K.Strisovsky. General and Modular Strategy For Designing Potent, Selective, and Pharmacologically Compliant Inhibitors of Rhomboid Proteases. Cell Chem Biol V. 24 1523 2017.
ISSN: ESSN 2451-9456
PubMed: 29107700
DOI: 10.1016/J.CHEMBIOL.2017.09.007