Fluorine in PDB 5l4w: Crystal Structure of Fimh Lectin Domain in Complex with 3-Fluoro- Heptylmannoside

The structure of Crystal Structure of Fimh Lectin Domain in Complex with 3-Fluoro- Heptylmannoside, PDB code: 5l4w was solved by R.P.Jakob, P.Zihlmann, S.Rabbani, T.Maier, B.Ernst, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	68.18 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	44.830, 95.340, 70.800, 90.00, 105.64, 90.00
R / Rfree (%)	17.2 / 20.2

The binding sites of Fluorine atom in the Crystal Structure of Fimh Lectin Domain in Complex with 3-Fluoro- Heptylmannoside (pdb code 5l4w). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of Fimh Lectin Domain in Complex with 3-Fluoro- Heptylmannoside, PDB code: 5l4w:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of Fimh Lectin Domain in Complex with 3-Fluoro- Heptylmannoside


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Fimh Lectin Domain in Complex with 3-Fluoro- Heptylmannoside within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:26.5 occ:1.00 F3 A:6KH301 0.0 26.5 1.0 C3 A:6KH301 1.4 23.6 1.0 C4 A:6KH301 2.4 23.2 1.0 C2 A:6KH301 2.4 25.2 1.0 O2 A:6KH301 2.7 26.4 1.0 O4 A:6KH301 2.8 21.7 1.0 NE2 A:GLN133 3.0 19.1 1.0 OD2 A:ASP140 3.2 26.2 1.0 CE2 A:PHE142 3.4 23.6 1.0 OE1 A:GLN133 3.5 20.8 1.0 CB A:ASP140 3.6 24.8 1.0 O A:HOH413 3.7 17.1 1.0 CD A:GLN133 3.7 24.8 1.0 C5 A:6KH301 3.7 25.1 1.0 C1 A:6KH301 3.7 23.0 1.0 CD2 A:PHE142 3.8 21.2 1.0 ND2 A:ASN135 3.8 21.4 1.0 CG A:ASP140 3.8 28.5 1.0 O5 A:6KH301 4.1 22.2 1.0 O1 A:6KH301 4.3 26.2 1.0 CZ A:PHE142 4.6 22.7 1.0 CB A:PHE1 4.6 17.8 1.0 OD1 A:ASP54 4.8 22.6 1.0 N A:PHE1 4.9 17.1 1.0 C6 A:6KH301 4.9 25.4 1.0 CG A:ASN135 5.0 28.0 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of Fimh Lectin Domain in Complex with 3-Fluoro- Heptylmannoside


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of Fimh Lectin Domain in Complex with 3-Fluoro- Heptylmannoside within 5.0Å range: probe atom residue distance (Å) B Occ B:F301 b:17.9 occ:1.00 F3 B:6KH301 0.0 17.9 1.0 C3 B:6KH301 1.4 18.7 1.0 C4 B:6KH301 2.4 18.0 1.0 C2 B:6KH301 2.4 20.4 1.0 O2 B:6KH301 2.7 20.5 1.0 O4 B:6KH301 2.8 16.3 1.0 NE2 B:GLN133 3.0 15.3 1.0 OD2 B:ASP140 3.3 25.5 1.0 CE2 B:PHE142 3.4 21.8 1.0 OE1 B:GLN133 3.5 21.6 1.0 CB B:ASP140 3.6 22.8 1.0 O B:HOH419 3.6 18.6 1.0 CD B:GLN133 3.7 18.1 1.0 C5 B:6KH301 3.7 18.8 1.0 C1 B:6KH301 3.8 21.8 1.0 CD2 B:PHE142 3.8 19.7 1.0 CG B:ASP140 3.8 27.7 1.0 ND2 B:ASN135 3.8 18.5 1.0 O5 B:6KH301 4.1 21.6 1.0 O1 B:6KH301 4.3 22.7 1.0 CZ B:PHE142 4.6 19.6 1.0 CB B:PHE1 4.6 17.1 1.0 O B:HOH423 4.7 30.9 1.0 OD1 B:ASP54 4.7 20.4 1.0 N B:PHE1 4.9 17.8 1.0 C6 B:6KH301 4.9 16.9 1.0 CG B:ASN135 4.9 22.8 1.0 CA B:ASP140 5.0 22.3 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of Fimh Lectin Domain in Complex with 3-Fluoro- Heptylmannoside


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of Fimh Lectin Domain in Complex with 3-Fluoro- Heptylmannoside within 5.0Å range: probe atom residue distance (Å) B Occ C:F301 b:22.2 occ:1.00 F3 C:6KH301 0.0 22.2 1.0 C3 C:6KH301 1.4 21.7 1.0 C4 C:6KH301 2.4 22.2 1.0 C2 C:6KH301 2.4 21.0 1.0 O2 C:6KH301 2.8 23.1 1.0 O4 C:6KH301 2.8 21.3 1.0 NE2 C:GLN133 3.0 14.8 1.0 OD2 C:ASP140 3.3 41.9 1.0 CE2 C:PHE142 3.4 23.9 1.0 OE1 C:GLN133 3.5 18.5 1.0 CB C:ASP140 3.6 21.9 1.0 O C:HOH414 3.6 19.2 1.0 CD C:GLN133 3.7 24.3 1.0 C1 C:6KH301 3.7 21.6 1.0 C5 C:6KH301 3.7 22.6 1.0 CD2 C:PHE142 3.7 20.9 1.0 ND2 C:ASN135 3.8 23.1 1.0 CG C:ASP140 3.9 32.8 1.0 O5 C:6KH301 4.1 21.0 1.0 O1 C:6KH301 4.2 22.9 1.0 CZ C:PHE142 4.6 22.4 1.0 CB C:PHE1 4.6 16.4 1.0 OD1 C:ASP54 4.8 20.8 1.0 N C:PHE1 4.9 16.1 1.0 C6 C:6KH301 4.9 21.6 1.0 CG C:ASN135 4.9 27.2 1.0

P.Zihlmann, X.Jiang, C.P.Sager, B.Fiege, R.P.Jakob, S.Siegrist, A.Zalewski, S.Rabbani, D.Eris, M.Silbermann, L.Pang, T.Muhlethaler, T.Sharpe, T.Maier, B.Ernst. High-Affinity Carbohydrate-Lectin Interactions: How Nature Makes It Possible To Be Published.