Fluorine in PDB 8pgn: Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 3169

Protein crystallography data

The structure of Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 3169, PDB code: 8pgn was solved by K.Calvopina, J.Brem, A.J.M.Farley, M.D.Allen, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.18 / 1.12
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 39.43, 67.95, 40.25, 90, 93.4, 90
R / Rfree (%) 12.1 / 14

Other elements in 8pgn:

The structure of Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 3169 also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 3169 (pdb code 8pgn). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 3169, PDB code: 8pgn:

Fluorine binding site 1 out of 1 in 8pgn

Go back to Fluorine Binding Sites List in 8pgn
Fluorine binding site 1 out of 1 in the Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 3169


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 the Metallo-Beta-Lactamase VIM1 with 3169 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F303

b:25.6
occ:1.00
F14 A:YRF303 0.0 25.6 1.0
C13 A:YRF303 1.4 23.5 1.0
C12 A:YRF303 2.4 19.1 1.0
HB2 A:HIS240 2.4 14.9 1.0
C15 A:YRF303 2.5 22.3 1.0
H121 A:YRF303 2.6 22.9 1.0
N16 A:YRF303 2.9 25.3 1.0
O A:HOH469 2.9 15.4 0.6
H182 A:YRF303 2.9 29.1 1.0
O A:HOH533 3.1 12.0 0.9
H161 A:YRF303 3.2 30.3 1.0
CB A:HIS240 3.2 12.4 1.0
H181 A:YRF303 3.2 29.1 1.0
HE1 A:HIS201 3.2 23.8 1.0
HB3 A:HIS240 3.3 14.9 1.0
C18 A:YRF303 3.4 24.2 1.0
O A:HOH664 3.5 19.1 0.6
C11 A:YRF303 3.7 16.3 1.0
CG A:HIS240 3.7 11.5 1.0
ND1 A:HIS201 3.8 18.7 1.0
C21 A:YRF303 3.8 21.8 1.0
CE1 A:HIS201 3.8 19.8 1.0
S17 A:YRF303 3.8 27.2 1.0
HD2 A:HIS240 3.9 14.2 1.0
CD2 A:HIS240 4.0 11.9 1.0
O A:HOH498 4.2 10.9 0.9
C22 A:YRF303 4.3 18.9 1.0
O A:HIS240 4.3 11.3 1.0
HA3 A:GLY209 4.3 23.8 1.0
O09 A:YRF303 4.4 14.8 1.0
H183 A:YRF303 4.4 29.1 1.0
HA2 A:GLY209 4.4 23.8 1.0
CA A:HIS240 4.5 11.4 1.0
O A:HOH547 4.6 10.9 0.6
ND1 A:HIS240 4.6 12.2 1.0
C A:HIS240 4.6 10.7 1.0
H211 A:YRF303 4.7 26.1 1.0
C07 A:YRF303 4.7 13.2 1.0
H A:HIS240 4.7 11.5 1.0
O20 A:YRF303 4.8 27.6 1.0
O19 A:YRF303 4.8 27.7 1.0
O A:HOH643 4.8 27.8 0.5
C10 A:YRF303 4.8 13.2 1.0
CA A:GLY209 4.9 19.9 1.0
HD1 A:HIS240 4.9 14.7 0.7
N A:HIS240 5.0 9.6 1.0

Reference:

K.Calvopina, J.Brem, A.J.M.Farley, M.D.Allen, C.J.Schofield. Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 3169 To Be Published.
Page generated: Fri Aug 2 22:08:06 2024

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