Chlorine in PDB 7ayn: Crystal Structure of the Lectin Domain of the Fimh Variant ARG98ALA, in Complex with Methyl 3-Chloro-4-D-Mannopyranosyloxy-3- Biphenylcarboxylate

The structure of Crystal Structure of the Lectin Domain of the Fimh Variant ARG98ALA, in Complex with Methyl 3-Chloro-4-D-Mannopyranosyloxy-3- Biphenylcarboxylate, PDB code: 7ayn was solved by R.P.Jakob, T.Tomasic, S.Rabbani, A.Reisner, Z.Jakopin, T.Maier, B.Ernst, M.Anderluh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.30 / 1.42
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	54.652, 32.926, 177.442, 90.00, 96.56, 90.00
R / Rfree (%)	15.9 / 18.4

The binding sites of Chlorine atom in the Crystal Structure of the Lectin Domain of the Fimh Variant ARG98ALA, in Complex with Methyl 3-Chloro-4-D-Mannopyranosyloxy-3- Biphenylcarboxylate (pdb code 7ayn). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of the Lectin Domain of the Fimh Variant ARG98ALA, in Complex with Methyl 3-Chloro-4-D-Mannopyranosyloxy-3- Biphenylcarboxylate, PDB code: 7ayn:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Crystal Structure of the Lectin Domain of the Fimh Variant ARG98ALA, in Complex with Methyl 3-Chloro-4-D-Mannopyranosyloxy-3- Biphenylcarboxylate


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 the Lectin Domain of the Fimh Variant ARG98ALA, in Complex with Methyl 3-Chloro-4-D-Mannopyranosyloxy-3- Biphenylcarboxylate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:14.9 occ:1.00 CL A:SBQ301 0.0 14.9 1.0 C19 A:SBQ301 1.7 10.0 1.0 C18 A:SBQ301 2.7 12.5 1.0 C6 A:SBQ301 2.7 9.8 1.0 H13 B:SBQ301 2.8 15.3 1.0 H20 A:SBQ301 2.8 15.0 1.0 O5 A:SBQ301 2.8 11.4 1.0 HE2 A:TYR137 3.3 18.3 1.0 HD11 A:ILE52 3.3 12.8 1.0 H20 B:SBQ301 3.4 14.1 1.0 C18 B:SBQ301 3.6 11.7 1.0 O B:HOH481 3.7 23.4 1.0 HD13 A:ILE52 3.7 12.8 1.0 HD2 A:TYR137 3.7 16.9 1.0 CE2 A:TYR137 3.7 15.2 1.0 C11 B:SBQ301 3.7 12.8 1.0 HD12 A:ILE52 3.7 12.8 1.0 H3 A:SBQ301 3.8 11.2 1.0 CD1 A:ILE52 3.8 10.7 1.0 H1 A:SBQ301 3.8 12.6 1.0 O A:HOH476 3.8 29.2 1.0 HD21 A:ASN138 3.9 16.0 1.0 HD22 A:ASN138 3.9 16.0 1.0 C7 A:SBQ301 4.0 10.4 1.0 C9 A:SBQ301 4.0 12.8 1.0 CD2 A:TYR137 4.0 14.1 1.0 C9 B:SBQ301 4.0 12.7 1.0 O A:HOH527 4.2 21.3 1.0 C19 B:SBQ301 4.2 10.2 1.0 ND2 A:ASN138 4.2 13.3 1.0 HD2 A:TYR48 4.2 18.1 1.0 C5 A:SBQ301 4.2 11.5 1.0 C10 B:SBQ301 4.3 12.6 1.0 C8 A:SBQ301 4.5 12.7 1.0 CL B:SBQ301 4.6 12.4 1.0 C3 A:SBQ301 4.7 9.3 1.0 CZ A:TYR137 4.7 15.8 1.0 C1 A:SBQ301 4.7 10.5 1.0 C12 B:SBQ301 4.7 14.4 1.0 H A:SBQ301 4.7 11.9 1.0 H14 B:SBQ301 4.8 17.4 1.0 O4 A:SBQ301 4.8 10.3 1.0 C A:SBQ301 4.8 9.9 1.0 C8 B:SBQ301 4.8 11.3 1.0 H11 A:SBQ301 4.9 12.6 1.0 H7 A:SBQ301 4.9 12.2 1.0 H4 A:SBQ301 4.9 13.9 1.0 H13 A:SBQ301 4.9 30.5 1.0 C6 B:SBQ301 4.9 10.2 1.0

Chlorine binding site 2 out of 4 in the Crystal Structure of the Lectin Domain of the Fimh Variant ARG98ALA, in Complex with Methyl 3-Chloro-4-D-Mannopyranosyloxy-3- Biphenylcarboxylate


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 the Lectin Domain of the Fimh Variant ARG98ALA, in Complex with Methyl 3-Chloro-4-D-Mannopyranosyloxy-3- Biphenylcarboxylate within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl301 b:12.4 occ:1.00 CL B:SBQ301 0.0 12.4 1.0 C19 B:SBQ301 1.7 10.2 1.0 C18 B:SBQ301 2.7 11.7 1.0 C6 B:SBQ301 2.7 10.2 1.0 H13 A:SBQ301 2.8 30.5 1.0 H20 B:SBQ301 2.8 14.1 1.0 O5 B:SBQ301 2.9 11.4 1.0 HE2 B:TYR137 3.3 21.0 1.0 HD11 B:ILE52 3.3 15.3 1.0 H20 A:SBQ301 3.5 15.0 1.0 O A:HOH476 3.7 29.2 1.0 H3 B:SBQ301 3.7 13.6 1.0 H1 B:SBQ301 3.7 14.3 1.0 HD13 B:ILE52 3.7 15.3 1.0 HD22 B:ASN138 3.8 21.2 1.0 O B:HOH481 3.8 23.4 1.0 HD12 B:ILE52 3.8 15.3 1.0 CE2 B:TYR137 3.8 17.5 1.0 HD21 B:ASN138 3.8 21.2 1.0 CD1 B:ILE52 3.8 12.7 1.0 HD2 B:TYR137 3.8 19.9 1.0 C18 A:SBQ301 3.8 12.5 1.0 C11 A:SBQ301 3.8 25.4 1.0 C9 B:SBQ301 4.0 12.7 1.0 C7 B:SBQ301 4.0 11.7 1.0 ND2 B:ASN138 4.0 17.6 1.0 CD2 B:TYR137 4.1 16.6 1.0 O B:HOH521 4.1 25.5 1.0 C5 B:SBQ301 4.2 10.0 1.0 HD2 B:TYR48 4.3 14.7 1.0 C19 A:SBQ301 4.3 10.0 1.0 C9 A:SBQ301 4.3 12.8 1.0 C8 B:SBQ301 4.5 11.3 1.0 C10 A:SBQ301 4.5 14.4 1.0 CL A:SBQ301 4.6 14.9 1.0 C3 B:SBQ301 4.6 11.3 1.0 C1 B:SBQ301 4.6 11.9 1.0 H14 A:SBQ301 4.7 29.5 1.0 H B:SBQ301 4.7 13.1 1.0 CZ B:TYR137 4.7 17.2 1.0 C12 A:SBQ301 4.8 24.5 1.0 H7 B:SBQ301 4.8 14.3 1.0 C B:SBQ301 4.8 10.9 1.0 O4 B:SBQ301 4.8 11.0 1.0 H13 B:SBQ301 4.8 15.3 1.0 H11 B:SBQ301 4.8 14.0 1.0 H4 B:SBQ301 4.9 12.0 1.0

Chlorine binding site 3 out of 4 in the Crystal Structure of the Lectin Domain of the Fimh Variant ARG98ALA, in Complex with Methyl 3-Chloro-4-D-Mannopyranosyloxy-3- Biphenylcarboxylate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of the Lectin Domain of the Fimh Variant ARG98ALA, in Complex with Methyl 3-Chloro-4-D-Mannopyranosyloxy-3- Biphenylcarboxylate within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl301 b:20.1 occ:1.00 CL C:SBQ301 0.0 20.1 1.0 C19 C:SBQ301 1.7 18.9 1.0 C18 C:SBQ301 2.7 16.4 1.0 C6 C:SBQ301 2.7 19.2 1.0 H20 C:SBQ301 2.8 19.8 1.0 H13 D:SBQ301 2.9 53.1 1.0 O5 C:SBQ301 2.9 18.4 1.0 HE2 C:TYR137 3.3 33.2 1.0 HD11 C:ILE52 3.3 24.1 1.0 H20 D:SBQ301 3.5 21.4 1.0 HD21 C:ASN138 3.6 39.1 1.0 HD22 C:ASN138 3.6 39.1 1.0 O C:HOH486 3.6 35.7 1.0 HD13 C:ILE52 3.7 24.1 1.0 H1 C:SBQ301 3.7 17.1 1.0 H3 C:SBQ301 3.7 15.5 1.0 HD2 C:TYR137 3.7 33.9 1.0 C18 D:SBQ301 3.8 17.8 1.0 CD1 C:ILE52 3.8 20.1 1.0 HD12 C:ILE52 3.8 24.1 1.0 ND2 C:ASN138 3.9 32.6 1.0 CE2 C:TYR137 3.9 27.6 1.0 C11 D:SBQ301 3.9 44.3 1.0 C9 C:SBQ301 4.0 17.8 1.0 C7 C:SBQ301 4.0 17.3 1.0 O C:HOH478 4.0 38.2 1.0 CD2 C:TYR137 4.1 28.2 1.0 C19 D:SBQ301 4.3 17.8 1.0 C5 C:SBQ301 4.3 14.0 1.0 C9 D:SBQ301 4.3 17.7 1.0 O D:HOH454 4.4 70.4 1.0 HD2 C:TYR48 4.4 25.6 1.0 C8 C:SBQ301 4.5 17.6 1.0 CL D:SBQ301 4.6 22.1 1.0 C10 D:SBQ301 4.6 23.4 1.0 C3 C:SBQ301 4.6 12.8 1.0 C1 C:SBQ301 4.6 14.2 1.0 H C:SBQ301 4.7 20.0 1.0 H7 C:SBQ301 4.7 19.0 1.0 C C:SBQ301 4.8 16.7 1.0 H14 D:SBQ301 4.8 48.9 1.0 O4 C:SBQ301 4.8 15.9 1.0 H13 C:SBQ301 4.8 27.3 1.0 C12 D:SBQ301 4.9 40.7 1.0 H11 C:SBQ301 4.9 20.8 1.0 CZ C:TYR137 4.9 26.7 1.0 H4 C:SBQ301 5.0 16.8 1.0 OD2 C:ASP140 5.0 26.3 1.0

Chlorine binding site 4 out of 4 in the Crystal Structure of the Lectin Domain of the Fimh Variant ARG98ALA, in Complex with Methyl 3-Chloro-4-D-Mannopyranosyloxy-3- Biphenylcarboxylate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of the Lectin Domain of the Fimh Variant ARG98ALA, in Complex with Methyl 3-Chloro-4-D-Mannopyranosyloxy-3- Biphenylcarboxylate within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl301 b:22.1 occ:1.00 CL D:SBQ301 0.0 22.1 1.0 C19 D:SBQ301 1.7 17.8 1.0 C18 D:SBQ301 2.7 17.8 1.0 C6 D:SBQ301 2.7 17.7 1.0 H13 C:SBQ301 2.8 27.3 1.0 H20 D:SBQ301 2.8 21.4 1.0 O5 D:SBQ301 2.9 19.3 1.0 HE2 D:TYR137 3.3 33.2 1.0 HD11 D:ILE52 3.3 30.5 1.0 H20 C:SBQ301 3.4 19.8 1.0 C18 C:SBQ301 3.6 16.4 1.0 HD13 D:ILE52 3.7 30.5 1.0 CE2 D:TYR137 3.7 27.6 1.0 HD12 D:ILE52 3.7 30.5 1.0 C11 C:SBQ301 3.8 22.8 1.0 CD1 D:ILE52 3.8 25.4 1.0 H3 D:SBQ301 3.8 19.3 1.0 H1 D:SBQ301 3.8 20.8 1.0 HD2 D:TYR137 3.8 32.5 1.0 O C:HOH478 3.9 38.2 1.0 C7 D:SBQ301 4.0 18.4 1.0 C9 C:SBQ301 4.0 17.8 1.0 C9 D:SBQ301 4.0 17.7 1.0 HD21 D:ASN138 4.0 34.3 1.0 HD22 D:ASN138 4.0 34.3 1.0 CD2 D:TYR137 4.1 27.0 1.0 C19 C:SBQ301 4.1 18.9 1.0 C5 D:SBQ301 4.2 15.9 1.0 C10 C:SBQ301 4.3 20.5 1.0 HD2 D:TYR48 4.3 31.5 1.0 ND2 D:ASN138 4.3 28.6 1.0 O D:HOH507 4.5 30.7 1.0 C8 D:SBQ301 4.5 17.0 1.0 O D:HOH454 4.5 70.4 1.0 CL C:SBQ301 4.6 20.1 1.0 CZ D:TYR137 4.7 31.7 1.0 C3 D:SBQ301 4.7 16.0 1.0 C1 D:SBQ301 4.7 17.3 1.0 H D:SBQ301 4.8 23.2 1.0 C12 C:SBQ301 4.8 22.9 1.0 C8 C:SBQ301 4.8 17.6 1.0 O4 D:SBQ301 4.8 17.0 1.0 C D:SBQ301 4.8 19.3 1.0 H14 C:SBQ301 4.8 27.5 1.0 H11 D:SBQ301 4.8 22.1 1.0 C6 C:SBQ301 4.9 19.2 1.0 H4 D:SBQ301 4.9 19.1 1.0 H7 D:SBQ301 4.9 21.1 1.0 H13 D:SBQ301 5.0 53.1 1.0 OH D:TYR137 5.0 37.1 1.0

T.Tomasic, S.Rabbani, R.P.Jakob, A.Reisner, Z.Jakopin, T.Maier, B.Ernst, M.Anderluh. Does Targeting ARG98 of Fimh Lead to High Affinity Antagonists? Eur.J.Med.Chem. 2020.
ISSN: ISSN 0223-5234
DOI: 10.1016/J.EJMECH.2020.113093