Chlorine in PDB 6xi9: X-Ray Crystal Structure of Mqne From Pedobacter Heparinus in Complex with Aminofutalosine and Methionine

Enzymatic activity of X-Ray Crystal Structure of Mqne From Pedobacter Heparinus in Complex with Aminofutalosine and Methionine

All present enzymatic activity of X-Ray Crystal Structure of Mqne From Pedobacter Heparinus in Complex with Aminofutalosine and Methionine:
2.5.1.120;

Protein crystallography data

The structure of X-Ray Crystal Structure of Mqne From Pedobacter Heparinus in Complex with Aminofutalosine and Methionine, PDB code: 6xi9 was solved by T.L.Grove, J.B.Bonanno, S.C.Almo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.96 / 2.14
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 72.512, 75.079, 83.269, 90.00, 107.13, 90.00
R / Rfree (%) 15.1 / 19.8

Other elements in 6xi9:

The structure of X-Ray Crystal Structure of Mqne From Pedobacter Heparinus in Complex with Aminofutalosine and Methionine also contains other interesting chemical elements:

Iron (Fe) 8 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the X-Ray Crystal Structure of Mqne From Pedobacter Heparinus in Complex with Aminofutalosine and Methionine (pdb code 6xi9). 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 X-Ray Crystal Structure of Mqne From Pedobacter Heparinus in Complex with Aminofutalosine and Methionine, PDB code: 6xi9:

Chlorine binding site 1 out of 1 in 6xi9

Go back to Chlorine Binding Sites List in 6xi9
Chlorine binding site 1 out of 1 in the X-Ray Crystal Structure of Mqne From Pedobacter Heparinus in Complex with Aminofutalosine and Methionine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of X-Ray Crystal Structure of Mqne From Pedobacter Heparinus in Complex with Aminofutalosine and Methionine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl404

b:37.3
occ:1.00
 OG1 A:THR125 3.2 32.3 1.0
C9 A:V47403 3.4 27.7 1.0
NE2 A:HIS123 3.5 32.1 1.0
CG2 A:THR157 3.5 19.2 1.0
O1 A:V47403 3.5 25.9 1.0
CA A:GLY190 3.6 20.1 1.0
CG A:PRO188 3.6 23.2 1.0
CB A:PRO188 3.6 22.0 1.0
N A:GLY190 3.6 19.3 1.0
C8 A:V47403 3.6 26.3 1.0
C7 A:V47403 3.7 25.1 1.0
CB A:THR125 3.8 26.7 1.0
C10 A:V47403 3.9 30.1 1.0
C16 A:V47403 4.0 31.5 1.0
CG2 A:THR125 4.0 25.9 1.0
CE1 A:HIS123 4.1 30.3 1.0
CG A:MET402 4.2 26.3 1.0
CB A:MET402 4.6 24.0 1.0
CD2 A:HIS123 4.7 29.9 1.0
N A:GLY189 4.7 22.2 1.0
C A:PRO188 4.7 22.5 1.0
C A:GLY190 4.8 19.5 1.0
CA A:PRO188 4.8 21.8 1.0
C A:GLY189 4.9 20.6 1.0
C11 A:V47403 5.0 32.0 1.0

Reference:

A.G.Carl, L.D.Harris, M.Feng, L.U.Nordstrom, G.J.Gerfen, G.B.Evans, A.Silakov, S.C.Almo, T.L.Grove. Narrow-Spectrum Antibiotic Targeting of the Radical Sam Enzyme Mqne in Menaquinone Biosynthesis. Biochemistry V. 59 2562 2020.
ISSN: ISSN 0006-2960
PubMed: 32627538
DOI: 10.1021/ACS.BIOCHEM.0C00070
Page generated: Sat Dec 12 14:35:42 2020

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