Fluorine in PDB 5fr0: The Details of Glycolipid Glycan Hydrolysis By the Structural Analysis of A Family 123 Glycoside Hydrolase From Clostridium Perfringens

The structure of The Details of Glycolipid Glycan Hydrolysis By the Structural Analysis of A Family 123 Glycoside Hydrolase From Clostridium Perfringens, PDB code: 5fr0 was solved by I.Noach, B.Pluvinage, C.Laurie, K.T.Abe, M.Alteen, D.J.Vocadlo, A.B.Boraston, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	95.31 / 1.75
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	99.530, 99.530, 95.310, 90.00, 90.00, 120.00
R / Rfree (%)	18.074 / 22.099

The binding sites of Fluorine atom in the The Details of Glycolipid Glycan Hydrolysis By the Structural Analysis of A Family 123 Glycoside Hydrolase From Clostridium Perfringens (pdb code 5fr0). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the The Details of Glycolipid Glycan Hydrolysis By the Structural Analysis of A Family 123 Glycoside Hydrolase From Clostridium Perfringens, PDB code: 5fr0:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the The Details of Glycolipid Glycan Hydrolysis By the Structural Analysis of A Family 123 Glycoside Hydrolase From Clostridium Perfringens


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of The Details of Glycolipid Glycan Hydrolysis By the Structural Analysis of A Family 123 Glycoside Hydrolase From Clostridium Perfringens within 5.0Å range: probe atom residue distance (Å) B Occ A:F1585 b:60.4 occ:1.00 F2 A:SIZ1585 0.0 60.4 1.0 C8 A:SIZ1585 1.2 52.4 1.0 F1 A:SIZ1585 2.2 59.4 1.0 C7 A:SIZ1585 2.2 48.2 1.0 O7 A:SIZ1585 2.8 50.8 1.0 CD2 A:TYR423 3.1 26.8 1.0 CG A:TYR423 3.1 25.1 1.0 CE2 A:TYR423 3.2 27.8 1.0 CD1 A:TYR423 3.2 28.1 1.0 CZ A:TYR423 3.2 30.6 1.0 CE1 A:TYR423 3.2 29.7 1.0 N2 A:SIZ1585 3.2 46.3 1.0 CB A:ALA374 3.5 36.3 1.0 CD2 A:LEU457 3.7 24.4 1.0 O A:HOH2312 3.9 24.6 1.0 CB A:TYR423 4.0 21.1 1.0 OH A:TYR423 4.0 34.7 1.0 OD1 A:ASP344 4.4 39.4 1.0 C2 A:SIZ1585 4.5 42.1 1.0 OE2 A:GLU345 4.7 56.7 1.0 C1 A:SIZ1585 4.7 40.5 1.0 O1 A:SIZ1585 4.7 44.5 1.0 CA A:ALA374 4.8 34.8 1.0 CZ2 A:TRP180 4.9 35.0 1.0

Fluorine binding site 2 out of 2 in the The Details of Glycolipid Glycan Hydrolysis By the Structural Analysis of A Family 123 Glycoside Hydrolase From Clostridium Perfringens


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of The Details of Glycolipid Glycan Hydrolysis By the Structural Analysis of A Family 123 Glycoside Hydrolase From Clostridium Perfringens within 5.0Å range: probe atom residue distance (Å) B Occ A:F1585 b:59.4 occ:1.00 F1 A:SIZ1585 0.0 59.4 1.0 C8 A:SIZ1585 1.5 52.4 1.0 F2 A:SIZ1585 2.2 60.4 1.0 C7 A:SIZ1585 2.5 48.2 1.0 OD1 A:ASP344 2.5 39.4 1.0 N2 A:SIZ1585 2.7 46.3 1.0 CB A:ALA374 2.9 36.3 1.0 CG A:ASP344 3.1 36.4 1.0 CH2 A:TRP180 3.5 31.2 1.0 O7 A:SIZ1585 3.6 50.8 1.0 OD2 A:ASP344 3.6 32.4 1.0 CZ2 A:TRP180 3.7 35.0 1.0 CB A:ASP344 4.1 33.6 1.0 C2 A:SIZ1585 4.2 42.1 1.0 CA A:ASP344 4.3 36.1 1.0 CA A:ALA374 4.4 34.8 1.0 CG A:GLU345 4.5 49.8 1.0 CZ3 A:TRP180 4.6 33.3 1.0 O A:ALA374 4.7 36.6 1.0 CZ A:TYR423 4.7 30.6 1.0 CE2 A:TYR423 4.7 27.8 1.0 CD2 A:LEU457 4.7 24.4 1.0 N A:GLU345 4.7 40.0 1.0 C A:ALA374 4.7 35.2 1.0 OE2 A:GLU345 4.8 56.7 1.0 CD A:GLU345 4.8 54.9 1.0 C A:ASP344 4.8 34.2 1.0 C3 A:SIZ1585 4.9 37.8 1.0 CE2 A:TRP180 4.9 30.4 1.0 O3 A:SIZ1585 4.9 32.5 1.0 OH A:TYR284 4.9 37.3 1.0 OH A:TYR423 4.9 34.7 1.0 CE1 A:TYR423 5.0 29.7 1.0

I.Noach, B.Pluvinage, C.Laurie, K.T.Abe, M.Alteen, D.J.Vocadlo, A.B.Boraston. The Details of Glycolipid Glycan Hydrolysis By the Structural Analysis of A Family 123 Glycoside Hydrolase From Clostridium Perfringens J.Mol.Biol. V. 428 3253 2016.
ISSN: ISSN 0022-2836
PubMed: 27038508
DOI: 10.1016/J.JMB.2016.03.020