Fluorine in PDB 1exp: Beta-1,4-Glycanase Cex-Cd

All present enzymatic activity of Beta-1,4-Glycanase Cex-Cd:
3.2.1.8; 3.2.1.91;

The structure of Beta-1,4-Glycanase Cex-Cd, PDB code: 1exp was solved by A.White, D.Tull, K.L.Johns, S.G.Withers, D.R.Rose, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 1.80
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	88.172, 88.172, 81.097, 90.00, 90.00, 90.00
R / Rfree (%)	20.8 / 28.3

The binding sites of Fluorine atom in the Beta-1,4-Glycanase Cex-Cd (pdb code 1exp). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Beta-1,4-Glycanase Cex-Cd, PDB code: 1exp:

Fluorine binding site 1 out of 1 in the Beta-1,4-Glycanase Cex-Cd


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Beta-1,4-Glycanase Cex-Cd within 5.0Å range: probe atom residue distance (Å) B Occ A:F602 b:19.8 occ:0.75 F2 A:G2F602 0.0 19.8 0.8 C2 A:G2F602 1.4 30.5 0.8 C3 A:G2F602 2.6 34.7 0.8 C1 A:G2F602 2.6 29.0 0.8 ND2 A:ASN126 2.8 13.2 1.0 O3 A:G2F602 2.9 32.2 0.8 CE1 A:HIS80 3.0 20.0 1.0 OE2 A:GLU233 3.0 24.2 1.0 NE2 A:HIS80 3.1 22.6 1.0 OE1 A:GLU233 3.6 17.5 1.0 O5 A:G2F602 3.6 34.7 0.8 CG A:ASN126 3.7 12.6 1.0 CD A:GLU233 3.8 14.8 1.0 C4 A:G2F602 3.8 36.1 0.8 OD1 A:ASN126 3.8 20.7 1.0 OE2 A:GLU127 3.9 20.3 1.0 NE2 A:GLN203 3.9 14.0 1.0 CZ2 A:TRP84 4.0 20.9 1.0 CH2 A:TRP84 4.1 21.8 1.0 ND1 A:HIS80 4.2 22.0 1.0 CE2 A:TRP84 4.3 22.6 1.0 C5 A:G2F602 4.3 35.8 0.8 CD A:GLN203 4.4 13.6 1.0 CZ3 A:TRP84 4.5 24.6 1.0 OE1 A:GLN203 4.5 13.2 1.0 CD2 A:HIS80 4.5 21.7 1.0 ND2 A:ASN169 4.6 10.4 1.0 CD A:GLU127 4.6 17.7 1.0 CD2 A:TRP84 4.7 22.2 1.0 CE3 A:TRP84 4.8 23.7 1.0 NE1 A:TRP84 4.9 19.5 1.0 O4 A:G2F602 4.9 39.1 0.8 CB A:ASN126 5.0 13.1 1.0

A.White, D.Tull, K.Johns, S.G.Withers, D.R.Rose. Crystallographic Observation of A Covalent Catalytic Intermediate in A Beta-Glycosidase. Nat.Struct.Biol. V. 3 149 1996.
ISSN: ISSN 1072-8368
PubMed: 8564541
DOI: 10.1038/NSB0296-149