Chlorine in PDB 5oa4: Fe(II)/(Alpha)Ketoglutarate-Dependent Dioxygenase ASQJ_V72I Mutant in Complex with 4-Methoxycyclopeptin (1)

The structure of Fe(II)/(Alpha)Ketoglutarate-Dependent Dioxygenase ASQJ_V72I Mutant in Complex with 4-Methoxycyclopeptin (1), PDB code: 5oa4 was solved by M.Groll, A.Braeuer, V.R.I.Kaila, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 1.55
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	72.780, 120.910, 66.760, 90.00, 90.00, 90.00
R / Rfree (%)	13.9 / 16.8

The structure of Fe(II)/(Alpha)Ketoglutarate-Dependent Dioxygenase ASQJ_V72I Mutant in Complex with 4-Methoxycyclopeptin (1) also contains other interesting chemical elements:

Nickel

(Ni)

1 atom

The binding sites of Chlorine atom in the Fe(II)/(Alpha)Ketoglutarate-Dependent Dioxygenase ASQJ_V72I Mutant in Complex with 4-Methoxycyclopeptin (1) (pdb code 5oa4). 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 Fe(II)/(Alpha)Ketoglutarate-Dependent Dioxygenase ASQJ_V72I Mutant in Complex with 4-Methoxycyclopeptin (1), PDB code: 5oa4:

Chlorine binding site 1 out of 1 in the Fe(II)/(Alpha)Ketoglutarate-Dependent Dioxygenase ASQJ_V72I Mutant in Complex with 4-Methoxycyclopeptin (1)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Fe(II)/(Alpha)Ketoglutarate-Dependent Dioxygenase ASQJ_V72I Mutant in Complex with 4-Methoxycyclopeptin (1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl404 b:20.4 occ:1.00 O A:HOH720 2.6 43.4 1.0 OG1 A:THR172 2.9 21.9 1.0 NH2 A:ARG223 3.1 22.5 1.0 NH1 A:ARG223 3.6 22.0 1.0 CA A:GLY213 3.7 19.2 1.0 CD2 A:LEU225 3.7 24.0 1.0 CZ A:ARG223 3.8 22.3 1.0 CB A:THR172 3.9 21.0 1.0 CG2 A:THR172 3.9 20.9 1.0 CD2 A:LEU159 4.0 25.1 0.5 C3 A:TRS403 4.0 24.8 0.8 CA A:THR172 4.3 20.5 1.0 N A:GLY213 4.3 18.4 1.0 N A:THR172 4.5 20.5 1.0 CE2 A:PHE165 4.5 21.9 1.0 N A:TRS403 4.6 21.6 0.8 O A:HOH731 4.8 23.7 1.0 CZ A:PHE165 4.9 21.4 1.0 C A:TRS403 4.9 23.4 0.8 C A:CYS212 4.9 18.6 1.0 O A:GLY170 4.9 20.7 1.0 C A:GLY213 5.0 20.1 1.0 O A:CYS212 5.0 18.4 1.0

S.L.Mader, A.Brauer, M.Groll, V.R.I.Kaila. Catalytic Mechanism and Molecular Engineering of Quinolone Biosynthesis in Dioxygenase Asqj. Nat Commun V. 9 1168 2018.
ISSN: ESSN 2041-1723
PubMed: 29563492
DOI: 10.1038/S41467-018-03442-2