Fluorine in PDB 1c22: E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex

All present enzymatic activity of E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex:
3.4.11.18;

The structure of E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex, PDB code: 1c22 was solved by W.T.Lowther, Y.Zhang, P.B.Sampson, J.F.Honek, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.10 / 1.75
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	39.128, 67.604, 48.826, 90.00, 111.05, 90.00
R / Rfree (%)	n/a / n/a

The structure of E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex also contains other interesting chemical elements:

Cobalt	(Co)	2 atoms
Sodium	(Na)	1 atom

The binding sites of Fluorine atom in the E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex (pdb code 1c22). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex, PDB code: 1c22:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:F300 b:48.9 occ:1.00 FZ1 A:MF3300 0.0 48.9 1.0 CE A:MF3300 1.4 51.8 1.0 FZ2 A:MF3300 2.0 54.7 1.0 FZ3 A:MF3300 2.3 56.2 1.0 SD A:MF3300 2.5 44.9 1.0 CG A:MF3300 3.0 34.8 1.0 CD2 A:HIS79 3.3 31.4 1.0 NE2 A:HIS79 3.4 31.9 1.0 CG A:HIS79 3.5 28.2 1.0 CE1 A:HIS79 3.7 31.9 1.0 ND1 A:HIS79 3.8 31.4 1.0 CB A:MF3300 3.9 20.4 1.0 CZ3 A:TRP221 4.0 24.7 1.0 SG A:CYS70 4.0 19.6 1.0 CB A:HIS79 4.2 20.6 1.0 CE3 A:TRP221 4.3 24.2 1.0 CD1 A:TYR65 4.4 16.9 1.0 CE1 A:TYR65 4.7 18.5 1.0 CA A:HIS79 4.8 17.0 1.0

Fluorine binding site 2 out of 3 in the E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:F300 b:54.7 occ:1.00 FZ2 A:MF3300 0.0 54.7 1.0 CE A:MF3300 1.4 51.8 1.0 FZ1 A:MF3300 2.0 48.9 1.0 FZ3 A:MF3300 2.4 56.2 1.0 SD A:MF3300 2.5 44.9 1.0 CZ3 A:TRP221 3.1 24.7 1.0 CH2 A:TRP221 3.7 24.0 1.0 CD1 A:TYR65 3.7 16.9 1.0 CB A:TYR65 3.9 17.5 1.0 CE3 A:TRP221 3.9 24.2 1.0 CG A:TYR65 3.9 17.6 1.0 CG A:MF3300 3.9 34.8 1.0 CD2 A:TYR62 4.1 25.0 1.0 O A:TYR62 4.3 19.8 1.0 CE1 A:TYR65 4.6 18.5 1.0 CZ2 A:TRP221 4.8 22.6 1.0 CD2 A:TYR65 4.8 18.2 1.0 CE2 A:TYR62 4.9 23.1 1.0 CB A:TYR62 4.9 18.1 1.0 CB A:MF3300 4.9 20.4 1.0 CD2 A:TRP221 4.9 23.5 1.0 CG A:TYR62 5.0 21.7 1.0

Fluorine binding site 3 out of 3 in the E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:F300 b:56.2 occ:1.00 FZ3 A:MF3300 0.0 56.2 1.0 CE A:MF3300 1.4 51.8 1.0 FZ1 A:MF3300 2.3 48.9 1.0 FZ2 A:MF3300 2.4 54.7 1.0 SD A:MF3300 2.5 44.9 1.0 CG A:MF3300 3.0 34.8 1.0 SG A:CYS70 3.1 19.6 1.0 CD1 A:TYR65 3.4 16.9 1.0 CG A:TYR65 3.4 17.6 1.0 CE1 A:TYR65 3.6 18.5 1.0 CD2 A:TYR65 3.7 18.2 1.0 CZ A:TYR65 3.8 18.9 1.0 CE2 A:TYR65 3.9 16.8 1.0 CB A:CYS59 4.0 20.6 1.0 SG A:CYS59 4.0 21.6 1.0 CB A:TYR65 4.1 17.5 1.0 CB A:MF3300 4.4 20.4 1.0 OH A:TYR65 4.6 20.0 1.0 O A:HOH570 4.8 30.7 1.0 CA A:CYS59 4.8 17.6 1.0 CB A:CYS70 4.9 15.9 1.0 CD2 A:HIS79 4.9 31.4 1.0 O A:CYS59 4.9 14.9 1.0 CZ3 A:TRP221 4.9 24.7 1.0

W.T.Lowther, Y.Zhang, P.B.Sampson, J.F.Honek, B.W.Matthews. Insights Into the Mechanism of Escherichia Coli Methionine Aminopeptidase From the Structural Analysis of Reaction Products and Phosphorus-Based Transition-State Analogues. Biochemistry V. 38 14810 1999.
ISSN: ISSN 0006-2960
PubMed: 10555963
DOI: 10.1021/BI991711G