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Fluorine in PDB 5agj: Crystal Structure of the Leurs Editing Domain of Candida Albicans in Complex with the Adduct AN2690-Amp

Enzymatic activity of Crystal Structure of the Leurs Editing Domain of Candida Albicans in Complex with the Adduct AN2690-Amp

All present enzymatic activity of Crystal Structure of the Leurs Editing Domain of Candida Albicans in Complex with the Adduct AN2690-Amp:
6.1.1.4;

Protein crystallography data

The structure of Crystal Structure of the Leurs Editing Domain of Candida Albicans in Complex with the Adduct AN2690-Amp, PDB code: 5agj was solved by H.Zhao, A.Palencia, E.Seiradake, Z.Ghaemi, Z.Luthey-Schulten, S.Cusack, S.A.Martinis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.57 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 42.950, 59.260, 97.150, 90.00, 90.00, 90.00
R / Rfree (%) 17.854 / 23.541

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of the Leurs Editing Domain of Candida Albicans in Complex with the Adduct AN2690-Amp (pdb code 5agj). 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 Leurs Editing Domain of Candida Albicans in Complex with the Adduct AN2690-Amp, PDB code: 5agj:

Fluorine binding site 1 out of 1 in 5agj

Go back to Fluorine Binding Sites List in 5agj
Fluorine binding site 1 out of 1 in the Crystal Structure of the Leurs Editing Domain of Candida Albicans in Complex with the Adduct AN2690-Amp


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 Leurs Editing Domain of Candida Albicans in Complex with the Adduct AN2690-Amp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F1817

b:13.5
occ:1.00
 F A:ANZ1817 0.0 13.5 1.0
CE1 A:ANZ1817 1.3 13.2 1.0
CD1 A:ANZ1817 2.3 12.5 1.0
CZ A:ANZ1817 2.4 12.7 1.0
CB A:ASP418 3.2 11.7 1.0
C A:ASP418 3.2 11.4 1.0
O A:ASP418 3.3 11.4 1.0
N A:SER419 3.5 11.2 1.0
O A:HOH2025 3.5 18.3 1.0
CG A:ANZ1817 3.6 12.5 1.0
CE2 A:ANZ1817 3.7 12.9 1.0
NH1 A:ARG318 3.8 24.4 1.0
CA A:ASP418 3.8 11.6 1.0
CD A:ARG318 4.0 19.6 1.0
CA A:SER419 4.0 11.4 1.0
CB A:SER419 4.0 11.1 1.0
CG2 A:THR321 4.1 12.1 1.0
CD2 A:ANZ1817 4.2 12.4 1.0
OG1 A:THR321 4.3 11.7 1.0
CZ A:ARG318 4.3 22.0 1.0
NE A:ARG318 4.4 20.6 1.0
CB A:THR321 4.5 11.9 1.0
CG A:ASP418 4.6 12.0 1.0
CG1 A:VAL415 4.6 10.8 1.0
N A:ASP418 4.6 11.5 1.0
CB A:ARG318 4.7 15.8 1.0
O A:VAL415 4.7 10.3 1.0
CB A:VAL415 4.8 10.7 1.0
O A:HOH2165 4.8 17.1 1.0
CG A:ARG318 4.8 17.6 1.0
O A:HOH2109 4.8 27.8 1.0
CB A:ANZ1817 5.0 12.2 1.0

Reference:

H.Zhao, A.Palencia, E.Seiradake, Z.Ghaemi, S.Cusack, Z.Luthey-Schulten, S.Martinis. Analysis of the Resistance Mechanism of A Benzoxaborole Inhibitor Reveals Insight Into the Leucyl-Trna Synthetase Editing Mechanism. Acs Chem.Biol. V. 10 2277 2015.
ISSN: ISSN 1554-8929
PubMed: 26172575
DOI: 10.1021/ACSCHEMBIO.5B00291
Page generated: Sun Dec 13 12:18:11 2020

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