Chlorine in PDB 6g2r: Crystal Structure of Fimh in Complex with A Tetraflourinated Biphenyl Alpha D-Mannoside

The structure of Crystal Structure of Fimh in Complex with A Tetraflourinated Biphenyl Alpha D-Mannoside, PDB code: 6g2r was solved by R.P.Jakob, W.Schoenemann, J.Cramer, T.Muehlethaler, P.Daetwyler, P.Zihlmann, B.Fiege, C.P.Sager, M.Smiesko, S.Rabbani, D.Eris, O.Schwardt, T.Maier, B.Ernst, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	52.97 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.115, 60.800, 105.938, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 22.2

The structure of Crystal Structure of Fimh in Complex with A Tetraflourinated Biphenyl Alpha D-Mannoside also contains other interesting chemical elements:

Fluorine

(F)

8 atoms

The binding sites of Chlorine atom in the Crystal Structure of Fimh in Complex with A Tetraflourinated Biphenyl Alpha D-Mannoside (pdb code 6g2r). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Fimh in Complex with A Tetraflourinated Biphenyl Alpha D-Mannoside, PDB code: 6g2r:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Fimh in Complex with A Tetraflourinated Biphenyl Alpha D-Mannoside


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Fimh in Complex with A Tetraflourinated Biphenyl Alpha D-Mannoside within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:42.5 occ:1.00 CL1 A:EJK301 0.0 42.5 1.0 CAF A:EJK301 1.7 43.1 1.0 CAA A:EJK301 2.7 46.1 1.0 CAE A:EJK301 2.7 46.6 1.0 O1 A:EJK301 2.8 41.7 1.0 HAE A:EJK301 2.8 55.8 1.0 HE2 A:TYR137 2.9 48.0 1.0 HD2 A:TYR137 3.3 45.7 1.0 HD21 A:ASN138 3.4 39.2 1.0 HD22 A:ASN138 3.4 39.2 1.0 CE2 A:TYR137 3.5 40.0 1.0 H31 A:EJK301 3.5 41.5 1.0 ND2 A:ASN138 3.6 32.7 1.0 HD11 A:ILE52 3.7 35.0 1.0 CD2 A:TYR137 3.7 38.1 1.0 HD13 A:ILE52 3.8 35.0 1.0 CAK B:EJK301 3.8 49.7 1.0 H5 A:EJK301 3.8 40.6 1.0 CAB A:EJK301 4.0 46.5 1.0 CAD A:EJK301 4.0 46.8 1.0 FAK B:EJK301 4.0 51.2 1.0 CAJ B:EJK301 4.0 50.9 1.0 CD1 A:ILE52 4.1 29.2 1.0 CAL B:EJK301 4.2 46.3 1.0 C1 A:EJK301 4.2 37.5 1.0 HD12 A:ILE52 4.3 35.0 1.0 CBE B:EJK301 4.4 54.5 1.0 CAC A:EJK301 4.5 47.2 1.0 HH A:TYR137 4.5 53.2 1.0 C3 A:EJK301 4.5 34.6 1.0 CAI B:EJK301 4.6 45.4 1.0 HH B:TYR137 4.6 48.4 1.0 CZ A:TYR137 4.6 41.3 1.0 H21 A:EJK301 4.6 38.5 1.0 FAL B:EJK301 4.6 45.3 1.0 FAL A:EJK301 4.6 44.8 1.0 CAG B:EJK301 4.7 43.3 1.0 OD2 A:ASP140 4.7 37.4 1.0 C2 A:EJK301 4.7 32.1 1.0 CG A:ASN138 4.7 32.1 1.0 H1 A:EJK301 4.7 45.0 1.0 HAE B:EJK301 4.7 44.9 1.0 C5 A:EJK301 4.8 33.9 1.0 HAB A:EJK301 4.8 55.7 1.0 O5 A:EJK301 4.9 34.1 1.0 CAH B:EJK301 4.9 41.8 1.0 CG A:TYR137 5.0 38.4 1.0 NBF B:EJK301 5.0 56.2 1.0 OH A:TYR137 5.0 44.4 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Fimh in Complex with A Tetraflourinated Biphenyl Alpha D-Mannoside


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Fimh in Complex with A Tetraflourinated Biphenyl Alpha D-Mannoside within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl301 b:33.3 occ:1.00 CL1 B:EJK301 0.0 33.3 1.0 CAF B:EJK301 1.7 33.4 1.0 CAA B:EJK301 2.7 34.1 1.0 CAE B:EJK301 2.7 37.5 1.0 O1 B:EJK301 2.8 30.2 1.0 HAE B:EJK301 2.8 44.9 1.0 HD21 B:ASN138 3.0 32.6 1.0 HD22 B:ASN138 3.2 32.6 1.0 HE2 B:TYR137 3.2 43.3 1.0 ND2 B:ASN138 3.3 27.2 1.0 HD2 B:TYR137 3.4 40.6 1.0 H31 B:EJK301 3.5 29.0 1.0 CAK A:EJK301 3.6 43.1 1.0 O B:HOH426 3.6 46.9 1.0 HD13 B:ILE52 3.7 35.5 1.0 HD11 B:ILE52 3.8 35.5 1.0 CE2 B:TYR137 3.8 36.1 1.0 H5 B:EJK301 3.8 24.8 1.0 CAJ A:EJK301 3.8 44.1 1.0 FAK A:EJK301 3.8 42.4 1.0 CD2 B:TYR137 3.9 33.9 1.0 CAB B:EJK301 4.0 35.7 1.0 CAL A:EJK301 4.0 45.6 1.0 CAD B:EJK301 4.0 39.6 1.0 CD1 B:ILE52 4.1 29.6 1.0 C1 B:EJK301 4.2 26.0 1.0 CBE A:EJK301 4.2 43.2 1.0 OD2 B:ASP140 4.2 30.3 1.0 HD12 B:ILE52 4.3 35.5 1.0 CAI A:EJK301 4.3 42.8 1.0 CAG A:EJK301 4.4 45.4 1.0 FAL A:EJK301 4.4 44.8 1.0 C3 B:EJK301 4.4 24.2 1.0 CAC B:EJK301 4.5 37.7 1.0 CG B:ASN138 4.5 24.6 1.0 H21 B:EJK301 4.5 27.0 1.0 C2 B:EJK301 4.6 22.6 1.0 FAL B:EJK301 4.6 45.3 1.0 CAH A:EJK301 4.7 42.6 1.0 HAE A:EJK301 4.7 55.8 1.0 H1 B:EJK301 4.7 31.2 1.0 C5 B:EJK301 4.7 20.7 1.0 HD21 B:ASN135 4.8 28.7 1.0 NBF A:EJK301 4.8 43.5 1.0 HAB B:EJK301 4.8 42.8 1.0 HH A:TYR137 4.8 53.2 1.0 O5 B:EJK301 4.9 22.6 1.0 CZ B:TYR137 5.0 38.2 1.0 HH B:TYR137 5.0 48.4 1.0 HB3 B:ASN138 5.0 29.8 1.0

W.Schonemann, J.Cramer, T.Muhlethaler, B.Fiege, M.Silbermann, S.Rabbani, P.Datwyler, P.Zihlmann, R.P.Jakob, C.P.Sager, M.Smiesko, O.Schwardt, T.Maier, B.Ernst. Improvement of Aglycone Pi-Stacking Yields Nanomolar to Sub-Nanomolar Fimh Antagonists. Chemmedchem V. 14 749 2019.
ISSN: ESSN 1860-7187
PubMed: 30710416
DOI: 10.1002/CMDC.201900051