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Fluorine in PDB 2evc: Crystal Structure of E. Coli. Methionine Amino Peptidase in Complex with 5-(2-(Trifluoromethyl)Phenyl)Furan-2- Carboxylic Acid

Enzymatic activity of Crystal Structure of E. Coli. Methionine Amino Peptidase in Complex with 5-(2-(Trifluoromethyl)Phenyl)Furan-2- Carboxylic Acid

All present enzymatic activity of Crystal Structure of E. Coli. Methionine Amino Peptidase in Complex with 5-(2-(Trifluoromethyl)Phenyl)Furan-2- Carboxylic Acid:
3.4.11.18;

Protein crystallography data

The structure of Crystal Structure of E. Coli. Methionine Amino Peptidase in Complex with 5-(2-(Trifluoromethyl)Phenyl)Furan-2- Carboxylic Acid, PDB code: 2evc was solved by W.-J.Huang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 37.800, 60.200, 50.400, 90.00, 104.50, 90.00
R / Rfree (%) 21 / 22.9

Other elements in 2evc:

The structure of Crystal Structure of E. Coli. Methionine Amino Peptidase in Complex with 5-(2-(Trifluoromethyl)Phenyl)Furan-2- Carboxylic Acid also contains other interesting chemical elements:

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

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of E. Coli. Methionine Amino Peptidase in Complex with 5-(2-(Trifluoromethyl)Phenyl)Furan-2- Carboxylic Acid (pdb code 2evc). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of E. Coli. Methionine Amino Peptidase in Complex with 5-(2-(Trifluoromethyl)Phenyl)Furan-2- Carboxylic Acid, PDB code: 2evc:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in 2evc

Go back to Fluorine Binding Sites List in 2evc
Fluorine binding site 1 out of 3 in the Crystal Structure of E. Coli. Methionine Amino Peptidase in Complex with 5-(2-(Trifluoromethyl)Phenyl)Furan-2- Carboxylic Acid


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 E. Coli. Methionine Amino Peptidase in Complex with 5-(2-(Trifluoromethyl)Phenyl)Furan-2- Carboxylic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F999

b:17.8
occ:1.00
F1 A:FC3999 0.0 17.8 1.0
CL1 A:FC3999 1.3 19.8 1.0
F3 A:FC3999 2.1 17.7 1.0
F2 A:FC3999 2.1 19.2 1.0
C2 A:FC3999 2.3 18.1 1.0
C1 A:FC3999 2.9 18.6 1.0
CD A:FC3999 2.9 16.3 1.0
CG A:FC3999 3.1 13.9 1.0
CE2 A:PHE177 3.4 13.7 1.0
C3 A:FC3999 3.5 21.3 1.0
OA A:FC3999 3.7 13.8 1.0
SG A:CYS59 3.7 17.8 1.0
CZ A:PHE177 3.8 12.6 1.0
CB A:CYS59 3.8 17.7 1.0
CD2 A:TYR62 3.9 22.5 1.0
CA A:CYS59 3.9 18.2 1.0
CB A:FC3999 4.0 14.4 1.0
CA A:FC3999 4.2 14.2 1.0
C6 A:FC3999 4.3 19.5 1.0
O A:HOH1021 4.5 13.3 1.0
CD2 A:PHE177 4.6 11.6 1.0
CB A:TYR62 4.6 23.2 1.0
O A:CYS59 4.6 19.9 1.0
C4 A:FC3999 4.7 20.2 1.0
CG A:TYR62 4.7 23.0 1.0
CE2 A:TYR62 4.7 24.3 1.0
SG A:CYS70 4.7 12.4 1.0
C A:CYS59 4.8 19.9 1.0
O A:HOH1010 4.9 11.5 1.0
N A:CYS59 4.9 17.1 1.0
CG A:TYR65 4.9 19.5 1.0
CB A:TYR65 5.0 19.3 1.0
C5 A:FC3999 5.0 20.5 1.0

Fluorine binding site 2 out of 3 in 2evc

Go back to Fluorine Binding Sites List in 2evc
Fluorine binding site 2 out of 3 in the Crystal Structure of E. Coli. Methionine Amino Peptidase in Complex with 5-(2-(Trifluoromethyl)Phenyl)Furan-2- Carboxylic Acid


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 E. Coli. Methionine Amino Peptidase in Complex with 5-(2-(Trifluoromethyl)Phenyl)Furan-2- Carboxylic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F999

b:19.2
occ:1.00
F2 A:FC3999 0.0 19.2 1.0
CL1 A:FC3999 1.3 19.8 1.0
F1 A:FC3999 2.1 17.8 1.0
F3 A:FC3999 2.2 17.7 1.0
C2 A:FC3999 2.3 18.1 1.0
C3 A:FC3999 2.6 21.3 1.0
CB A:TYR65 2.9 19.3 1.0
CG A:TYR65 3.3 19.5 1.0
O A:CYS59 3.4 19.9 1.0
O A:TYR62 3.5 21.1 1.0
C1 A:FC3999 3.7 18.6 1.0
CB A:TYR62 3.7 23.2 1.0
CD2 A:TYR62 3.8 22.5 1.0
CD2 A:TYR65 3.8 17.9 1.0
CA A:CYS59 3.9 18.2 1.0
CD1 A:TYR65 4.0 17.4 1.0
C A:CYS59 4.0 19.9 1.0
C4 A:FC3999 4.0 20.2 1.0
CB A:CYS59 4.1 17.7 1.0
CG A:TYR62 4.2 23.0 1.0
C A:TYR62 4.3 23.3 1.0
CA A:TYR65 4.4 21.0 1.0
CD A:FC3999 4.4 16.3 1.0
CA A:TYR62 4.5 23.8 1.0
CG A:FC3999 4.7 13.9 1.0
N A:TYR65 4.7 22.4 1.0
CH2 A:TRP221 4.8 21.3 1.0
N A:TYR62 4.8 24.6 1.0
C6 A:FC3999 4.8 19.5 1.0
CZ3 A:TRP221 4.8 21.7 1.0
SG A:CYS59 4.8 17.8 1.0
CE2 A:TYR65 4.8 17.8 1.0
CE2 A:TYR62 4.9 24.3 1.0
C5 A:FC3999 4.9 20.5 1.0
CE1 A:TYR65 4.9 16.7 1.0
CE2 A:PHE177 4.9 13.7 1.0

Fluorine binding site 3 out of 3 in 2evc

Go back to Fluorine Binding Sites List in 2evc
Fluorine binding site 3 out of 3 in the Crystal Structure of E. Coli. Methionine Amino Peptidase in Complex with 5-(2-(Trifluoromethyl)Phenyl)Furan-2- Carboxylic Acid


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of E. Coli. Methionine Amino Peptidase in Complex with 5-(2-(Trifluoromethyl)Phenyl)Furan-2- Carboxylic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F999

b:17.7
occ:1.00
F3 A:FC3999 0.0 17.7 1.0
CL1 A:FC3999 1.3 19.8 1.0
F1 A:FC3999 2.1 17.8 1.0
F2 A:FC3999 2.2 19.2 1.0
C2 A:FC3999 2.3 18.1 1.0
CG A:FC3999 3.1 13.9 1.0
C1 A:FC3999 3.1 18.6 1.0
C3 A:FC3999 3.3 21.3 1.0
SG A:CYS70 3.3 12.4 1.0
CD A:FC3999 3.3 16.3 1.0
CG A:TYR65 3.6 19.5 1.0
CD1 A:TYR65 3.6 17.4 1.0
CD2 A:TYR65 3.9 17.9 1.0
CE1 A:TYR65 4.0 16.7 1.0
CB A:TYR65 4.0 19.3 1.0
CE2 A:TYR65 4.3 17.8 1.0
CB A:FC3999 4.3 14.4 1.0
CZ A:TYR65 4.3 17.4 1.0
C6 A:FC3999 4.4 19.5 1.0
CB A:CYS59 4.4 17.7 1.0
C4 A:FC3999 4.5 20.2 1.0
O A:HOH1021 4.5 13.3 1.0
OA A:FC3999 4.5 13.8 1.0
CD2 A:HIS79 4.6 12.5 1.0
SG A:CYS59 4.6 17.8 1.0
CZ3 A:TRP221 4.8 21.7 1.0
CG A:HIS79 4.9 13.3 1.0
NE2 A:HIS79 4.9 14.3 1.0
CA A:CYS59 5.0 18.2 1.0
C5 A:FC3999 5.0 20.5 1.0

Reference:

S.X.Xie, W.J.Huang, Z.Q.Ma, M.Huang, R.P.Hanzlik, Q.Z.Ye. Structural Analysis of Metalloform-Selective Inhibition of Methionine Aminopeptidase. Acta Crystallogr.,Sect.D V. 62 425 2006.
ISSN: ISSN 0907-4449
PubMed: 16552144
DOI: 10.1107/S0907444906003878
Page generated: Sun Dec 13 11:35:45 2020

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