Fluorine in PDB 2q94: E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A04

All present enzymatic activity of E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A04:
3.4.11.18;

The structure of E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A04, PDB code: 2q94 was solved by Q.-Z.Ye, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.91 / 1.63
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	38.199, 60.605, 50.624, 90.00, 104.80, 90.00
R / Rfree (%)	21.3 / 23.8

The structure of E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A04 also contains other interesting chemical elements:

Manganese	(Mn)	2 atoms
Sodium	(Na)	1 atom

The binding sites of Fluorine atom in the E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A04 (pdb code 2q94). 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 Mn-Form with Inhibitor A04, PDB code: 2q94:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A04


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 Mn-Form with Inhibitor A04 within 5.0Å range: probe atom residue distance (Å) B Occ A:F400 b:20.2 occ:1.00 FAN A:A04400 0.0 20.2 1.0 CAL A:A04400 1.3 20.3 1.0 FAO A:A04400 2.2 20.1 1.0 FAM A:A04400 2.2 19.3 1.0 OAS A:A04400 2.3 18.0 1.0 CAJ A:A04400 2.8 18.5 1.0 CAC A:A04400 3.1 18.1 1.0 CAG A:A04400 3.2 19.7 1.0 CAE A:A04400 3.2 17.7 1.0 CE2 A:PHE177 3.4 15.2 1.0 SG A:CYS59 3.7 20.2 1.0 CAI A:A04400 3.7 21.4 1.0 CZ A:PHE177 3.8 14.6 1.0 CD2 A:TYR62 3.9 22.5 1.0 OAP A:A04400 3.9 14.7 1.0 CB A:CYS59 4.0 19.7 1.0 CA A:CYS59 4.0 19.5 1.0 CAD A:A04400 4.0 17.3 1.0 CAK A:A04400 4.3 21.8 1.0 CAA A:A04400 4.4 16.9 1.0 CB A:TYR62 4.4 24.6 1.0 O A:HOH509 4.4 12.7 1.0 CG A:TYR62 4.5 22.8 1.0 CD2 A:PHE177 4.5 14.7 1.0 CE2 A:TYR62 4.6 24.0 1.0 O A:CYS59 4.7 20.3 1.0 CAF A:A04400 4.7 22.4 1.0 O A:HOH508 4.8 12.9 1.0 SG A:CYS70 4.8 13.7 1.0 C A:CYS59 4.8 21.1 1.0 N A:CYS59 4.9 17.6 1.0 CAH A:A04400 5.0 23.9 1.0

Fluorine binding site 2 out of 3 in the E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A04


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 Mn-Form with Inhibitor A04 within 5.0Å range: probe atom residue distance (Å) B Occ A:F400 b:20.1 occ:1.00 FAO A:A04400 0.0 20.1 1.0 CAL A:A04400 1.3 20.3 1.0 FAN A:A04400 2.2 20.2 1.0 FAM A:A04400 2.2 19.3 1.0 OAS A:A04400 2.3 18.0 1.0 CAJ A:A04400 2.8 18.5 1.0 CAI A:A04400 3.0 21.4 1.0 CB A:TYR65 3.2 20.3 1.0 CG A:TYR65 3.4 21.3 1.0 CB A:TYR62 3.5 24.6 1.0 O A:CYS59 3.5 20.3 1.0 O A:TYR62 3.5 22.8 1.0 CD2 A:TYR62 3.6 22.5 1.0 CAG A:A04400 3.9 19.7 1.0 CD2 A:TYR65 3.9 21.2 1.0 CG A:TYR62 4.0 22.8 1.0 CA A:CYS59 4.0 19.5 1.0 CD1 A:TYR65 4.1 20.3 1.0 C A:CYS59 4.2 21.1 1.0 CAF A:A04400 4.2 22.4 1.0 CB A:CYS59 4.3 19.7 1.0 C A:TYR62 4.3 26.0 1.0 CA A:TYR62 4.4 25.5 1.0 CAC A:A04400 4.5 18.1 1.0 CA A:TYR65 4.6 21.5 1.0 N A:TYR62 4.7 27.5 1.0 CAE A:A04400 4.7 17.7 1.0 CE2 A:TYR62 4.7 24.0 1.0 CE2 A:TYR65 4.8 20.8 1.0 CAK A:A04400 4.9 21.8 1.0 SG A:CYS59 4.9 20.2 1.0 N A:TYR65 4.9 22.9 1.0 CE1 A:TYR65 5.0 20.7 1.0 CE2 A:PHE177 5.0 15.2 1.0

Fluorine binding site 3 out of 3 in the E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A04


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 Mn-Form with Inhibitor A04 within 5.0Å range: probe atom residue distance (Å) B Occ A:F400 b:19.3 occ:1.00 FAM A:A04400 0.0 19.3 1.0 CAL A:A04400 1.3 20.3 1.0 FAN A:A04400 2.2 20.2 1.0 FAO A:A04400 2.2 20.1 1.0 OAS A:A04400 2.2 18.0 1.0 SG A:CYS70 3.3 13.7 1.0 CB A:CYS59 3.4 19.7 1.0 CD2 A:TYR65 3.4 21.2 1.0 CG A:TYR65 3.5 21.3 1.0 CAJ A:A04400 3.5 18.5 1.0 SG A:CYS59 3.6 20.2 1.0 CE2 A:TYR65 3.7 20.8 1.0 CD1 A:TYR65 3.9 20.3 1.0 CAE A:A04400 3.9 17.7 1.0 CA A:CYS59 3.9 19.5 1.0 O A:HOH509 4.0 12.7 1.0 CB A:TYR65 4.0 20.3 1.0 CZ A:TYR65 4.1 21.0 1.0 CE1 A:TYR65 4.1 20.7 1.0 O A:CYS59 4.2 20.3 1.0 CAI A:A04400 4.3 21.4 1.0 CAC A:A04400 4.3 18.1 1.0 CAG A:A04400 4.4 19.7 1.0 C A:CYS59 4.4 21.1 1.0 CAD A:A04400 4.8 17.3 1.0 OH A:TYR65 4.9 21.5 1.0 CB A:CYS70 5.0 11.2 1.0

Z.Q.Ma, S.X.Xie, Q.Q.Huang, F.J.Nan, T.D.Hurley, Q.Z.Ye. Structural Analysis of Inhibition of E. Coli Methionine Aminopeptidase: Implication of Loop Flexibility in Selective Inhibition of Bacterial Enzymes. Bmc Struct.Biol. V. 7 84 2007.
ISSN: ESSN 1472-6807
PubMed: 18093325
DOI: 10.1186/1472-6807-7-84