Fluorine in PDB 1afq: Crystal Structure of Bovine Gamma-Chymotrypsin Complexed with A Synthetic Inhibitor

All present enzymatic activity of Crystal Structure of Bovine Gamma-Chymotrypsin Complexed with A Synthetic Inhibitor:
3.4.21.1;

The structure of Crystal Structure of Bovine Gamma-Chymotrypsin Complexed with A Synthetic Inhibitor, PDB code: 1afq was solved by S.Sugio, A.Kashima, Y.Inoue, I.Maeda, T.Nose, Y.Shimohigashi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	5.00 / 1.80
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	69.840, 69.840, 97.360, 90.00, 90.00, 90.00
R / Rfree (%)	18.1 / 18.2

The binding sites of Fluorine atom in the Crystal Structure of Bovine Gamma-Chymotrypsin Complexed with A Synthetic Inhibitor (pdb code 1afq). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of Bovine Gamma-Chymotrypsin Complexed with A Synthetic Inhibitor, PDB code: 1afq:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of Bovine Gamma-Chymotrypsin Complexed with A Synthetic Inhibitor


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 Bovine Gamma-Chymotrypsin Complexed with A Synthetic Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:F304 b:20.2 occ:1.00 F B:0FG304 0.0 20.2 1.0 C4 B:0FG304 1.3 19.9 1.0 C3 B:0FG304 2.3 19.9 1.0 C5 B:0FG304 2.4 19.5 1.0 C2 B:0FG304 3.6 19.8 1.0 C6 B:0FG304 3.6 19.6 1.0 C11 B:0FG304 4.1 19.8 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of Bovine Gamma-Chymotrypsin Complexed with A Synthetic Inhibitor


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 Bovine Gamma-Chymotrypsin Complexed with A Synthetic Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ C:F301 b:23.8 occ:1.00 F C:0FG301 0.0 23.8 1.0 C4 C:0FG301 1.3 23.4 1.0 C3 C:0FG301 2.3 23.2 1.0 C5 C:0FG301 2.4 23.5 1.0 O C:HOH596 3.1 29.2 1.0 O C:SER190 3.2 14.6 1.0 CA C:GLY216 3.5 16.4 1.0 O C:HOH539 3.5 23.2 1.0 N C:SER217 3.5 17.8 1.0 C2 C:0FG301 3.6 23.3 1.0 OG C:SER189 3.6 16.0 1.0 C6 C:0FG301 3.6 23.5 1.0 C C:GLY216 3.8 17.2 1.0 O C:SER217 4.0 18.6 1.0 N C:GLY216 4.1 15.4 1.0 C C:SER190 4.1 14.8 1.0 C11 C:0FG301 4.1 23.8 1.0 CA C:GLY226 4.4 14.7 1.0 CA C:CYS220 4.4 17.9 1.0 CA C:SER217 4.5 18.4 1.0 O C:TRP215 4.5 14.8 1.0 C C:TRP215 4.5 14.9 1.0 CB C:SER217 4.7 18.6 1.0 N C:SER190 4.7 14.7 1.0 C C:SER217 4.7 18.7 1.0 SG C:CYS220 4.8 16.6 1.0 O C:GLY216 4.8 17.3 1.0 O C:HOH519 4.9 16.9 1.0 CB C:SER190 4.9 14.4 1.0 CA C:SER190 4.9 14.6 1.0 N C:CYS191 4.9 14.9 1.0 CA C:CYS191 4.9 15.2 1.0 CB C:CYS220 4.9 17.2 1.0

A.Kashima, Y.Inoue, S.Sugio, I.Maeda, T.Nose, Y.Shimohigashi. X-Ray Crystal Structure of A Dipeptide-Chymotrypsin Complex in An Inhibitory Interaction. Eur.J.Biochem. V. 255 12 1998.
ISSN: ISSN 0014-2956
PubMed: 9692896
DOI: 10.1046/J.1432-1327.1998.2550012.X