Chlorine in PDB 8g0n: Fphi, Staphylococcus Aureus Fluorophosphonate-Binding Serine Hydrolases I, Apo Form

Protein crystallography data

The structure of Fphi, Staphylococcus Aureus Fluorophosphonate-Binding Serine Hydrolases I, Apo Form, PDB code: 8g0n was solved by M.Fellner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.54 / 1.14
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.457, 60.742, 76.38, 90, 90, 90
R / Rfree (%) 13.2 / 14.5

Other elements in 8g0n:

The structure of Fphi, Staphylococcus Aureus Fluorophosphonate-Binding Serine Hydrolases I, Apo Form also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Fphi, Staphylococcus Aureus Fluorophosphonate-Binding Serine Hydrolases I, Apo Form (pdb code 8g0n). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Fphi, Staphylococcus Aureus Fluorophosphonate-Binding Serine Hydrolases I, Apo Form, PDB code: 8g0n:

Chlorine binding site 1 out of 1 in 8g0n

Go back to Chlorine Binding Sites List in 8g0n
Chlorine binding site 1 out of 1 in the Fphi, Staphylococcus Aureus Fluorophosphonate-Binding Serine Hydrolases I, Apo Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Fphi, Staphylococcus Aureus Fluorophosphonate-Binding Serine Hydrolases I, Apo Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl303

b:31.6
occ:1.00
O A:HOH402 2.9 30.9 1.0
O A:HOH514 2.9 16.0 1.0
HG A:SER94 2.9 25.7 0.7
HB2 A:LEU95 3.2 15.6 1.0
HG3 A:PRO118 3.3 19.6 1.0
HZ A:PHE165 3.4 28.5 1.0
H A:LEU95 3.5 15.3 1.0
HB3 A:SER94 3.6 15.3 0.3
OG A:SER94 3.6 21.4 0.7
HE2 A:LYS121 3.6 39.4 1.0
N A:LEU95 3.8 12.8 1.0
HB2 A:PHE25 3.8 17.1 1.0
HA A:LEU95 3.8 15.0 1.0
HG3 A:LYS121 3.8 33.7 1.0
HB3 A:PHE25 3.9 17.1 1.0
CB A:LEU95 4.0 13.0 1.0
CZ A:PHE165 4.1 23.8 1.0
HD3 A:PRO118 4.1 18.2 1.0
CA A:LEU95 4.1 12.5 1.0
HD11 A:LEU98 4.1 18.0 1.0
CG A:PRO118 4.1 16.3 1.0
HD12 A:LEU98 4.2 18.0 1.0
CB A:PHE25 4.3 14.2 1.0
HB3 A:SER94 4.3 23.1 0.7
HD3 A:LYS121 4.3 37.0 1.0
HG2 A:PRO118 4.4 19.6 1.0
C A:SER94 4.4 13.7 0.7
H A:PHE25 4.4 15.7 1.0
C A:SER94 4.4 12.6 0.3
HE1 A:PHE165 4.5 29.4 1.0
CB A:SER94 4.5 12.7 0.3
CE A:LYS121 4.5 32.8 1.0
CB A:SER94 4.5 19.3 0.7
CD A:PRO118 4.5 15.2 1.0
HD21 A:LEU126 4.5 28.8 1.0
HZ3 A:LYS121 4.5 40.8 1.0
HB3 A:LEU95 4.5 15.6 1.0
HH A:TYR195 4.6 26.1 1.0
HD2 A:PRO118 4.6 18.2 1.0
CG A:LYS121 4.6 28.0 1.0
HD2 A:PHE25 4.6 19.9 1.0
HD13 A:LEU95 4.6 18.1 1.0
CD1 A:LEU98 4.6 15.0 1.0
CE1 A:PHE165 4.6 24.5 1.0
CD A:LYS121 4.7 30.8 1.0
HB2 A:SER94 4.7 15.3 0.3
O A:HOH505 4.8 19.8 1.0
HG2 A:LYS121 4.8 33.7 1.0
HD23 A:LEU126 4.9 28.8 1.0
HD11 A:ILE169 4.9 26.5 1.0
HA A:SER94 4.9 18.3 0.7
CA A:SER94 4.9 15.2 0.7
CE2 A:PHE165 4.9 22.4 1.0
CA A:SER94 4.9 12.4 0.3
HE2 A:PHE165 4.9 26.9 1.0
NZ A:LYS121 4.9 34.0 1.0
HA A:SER94 5.0 14.9 0.3
HD22 A:LEU95 5.0 17.0 1.0

Reference:

M.Fellner, M.Fellner. N/A N/A.
Page generated: Tue Jul 30 09:51:56 2024

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