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Fluorine in PDB 7c7o: Crystal Structure of E.Coli Dna Gyrase B in Complex with 6-Fluoro-8- (Methylamino)-2-Oxo-1,2-Dihydroquinoline Derivative

Enzymatic activity of Crystal Structure of E.Coli Dna Gyrase B in Complex with 6-Fluoro-8- (Methylamino)-2-Oxo-1,2-Dihydroquinoline Derivative

All present enzymatic activity of Crystal Structure of E.Coli Dna Gyrase B in Complex with 6-Fluoro-8- (Methylamino)-2-Oxo-1,2-Dihydroquinoline Derivative:
5.6.2.2;

Protein crystallography data

The structure of Crystal Structure of E.Coli Dna Gyrase B in Complex with 6-Fluoro-8- (Methylamino)-2-Oxo-1,2-Dihydroquinoline Derivative, PDB code: 7c7o was solved by M.Kamitani, M.Mima, T.Takeuchi, F.Ushiyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 17.61 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 41.251, 67.585, 67.913, 90.00, 90.00, 90.00
R / Rfree (%) 17 / 22.7

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of E.Coli Dna Gyrase B in Complex with 6-Fluoro-8- (Methylamino)-2-Oxo-1,2-Dihydroquinoline Derivative (pdb code 7c7o). 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 E.Coli Dna Gyrase B in Complex with 6-Fluoro-8- (Methylamino)-2-Oxo-1,2-Dihydroquinoline Derivative, PDB code: 7c7o:

Fluorine binding site 1 out of 1 in 7c7o

Go back to Fluorine Binding Sites List in 7c7o
Fluorine binding site 1 out of 1 in the Crystal Structure of E.Coli Dna Gyrase B in Complex with 6-Fluoro-8- (Methylamino)-2-Oxo-1,2-Dihydroquinoline Derivative


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 Dna Gyrase B in Complex with 6-Fluoro-8- (Methylamino)-2-Oxo-1,2-Dihydroquinoline Derivative within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F301

b:22.7
occ:1.00
 F30 A:FKU301 0.0 22.7 1.0
C2 A:FKU301 1.3 21.2 1.0
C1 A:FKU301 2.3 20.6 1.0
C3 A:FKU301 2.4 20.2 1.0
CG2 A:VAL120 3.1 25.4 1.0
CB A:VAL120 3.5 24.4 1.0
C6 A:FKU301 3.6 20.4 1.0
C4 A:FKU301 3.6 21.4 1.0
CG2 A:VAL167 3.8 14.7 1.0
CG1 A:VAL120 3.8 25.2 1.0
CB A:ASN46 4.0 21.5 1.0
CG1 A:VAL43 4.1 16.6 1.0
C5 A:FKU301 4.1 20.2 1.0
CG A:ASN46 4.2 22.5 1.0
ND2 A:ASN46 4.4 21.4 1.0
SD A:MET95 4.5 26.5 1.0
CB A:VAL167 4.6 15.0 1.0
N25 A:FKU301 4.7 21.1 1.0
CA A:VAL43 4.7 15.5 1.0
O A:VAL43 4.7 18.4 1.0
CE A:MET95 4.8 25.8 1.0
CB A:VAL43 4.8 15.8 1.0
OD1 A:ASN46 4.8 28.1 1.0
CG1 A:VAL167 4.9 15.4 1.0
C7 A:FKU301 4.9 21.5 1.0
CG2 A:VAL43 4.9 15.7 1.0
C22 A:FKU301 4.9 25.6 1.0
CA A:VAL120 4.9 22.7 1.0

Reference:

F.Ushiyama, H.Amada, Y.Mihara, T.Takeuchi, N.Tanaka-Yamamoto, M.Mima, M.Kamitani, R.Wada, Y.Tamura, M.Endo, A.Masuko, I.Takata, K.Hitaka, H.Sugiyama, N.Ohtake. Lead Optimization of 8-(Methylamino)-2-Oxo-1,2-Dihydroquinolines As Bacterial Type II Topoisomerase Inhibitors. Bioorg.Med.Chem. V. 28 15776 2020.
ISSN: ESSN 1464-3391
PubMed: 33032189
DOI: 10.1016/J.BMC.2020.115776
Page generated: Tue Jul 15 18:53:35 2025

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