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

Enzymatic activity of E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex

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

Protein crystallography data

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

Other elements in 1c22:

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

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

Fluorine Binding Sites:

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 1c22

Go back to Fluorine Binding Sites List in 1c22
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 1c22

Go back to Fluorine Binding Sites List in 1c22
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 1c22

Go back to Fluorine Binding Sites List in 1c22
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

Reference:

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
Page generated: Sun Dec 13 11:28:36 2020

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