Chlorine in PDB 6f2a: Crystal Structure of the Complex Fe(II)/Alpha-Ketoglutarate Dependent Dioxygenase KDO1 with Fe(II)/Lysine

The structure of Crystal Structure of the Complex Fe(II)/Alpha-Ketoglutarate Dependent Dioxygenase KDO1 with Fe(II)/Lysine, PDB code: 6f2a was solved by T.Isabet, E.A.Stura, P.Legrand, A.Zaparucha, K.Bastard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.16 / 2.00
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	56.940, 67.020, 110.750, 107.48, 102.76, 93.74
R / Rfree (%)	20.3 / 23.1

The structure of Crystal Structure of the Complex Fe(II)/Alpha-Ketoglutarate Dependent Dioxygenase KDO1 with Fe(II)/Lysine also contains other interesting chemical elements:

Iron

(Fe)

4 atoms

The binding sites of Chlorine atom in the Crystal Structure of the Complex Fe(II)/Alpha-Ketoglutarate Dependent Dioxygenase KDO1 with Fe(II)/Lysine (pdb code 6f2a). 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 Crystal Structure of the Complex Fe(II)/Alpha-Ketoglutarate Dependent Dioxygenase KDO1 with Fe(II)/Lysine, PDB code: 6f2a:

Chlorine binding site 1 out of 1 in the Crystal Structure of the Complex Fe(II)/Alpha-Ketoglutarate Dependent Dioxygenase KDO1 with Fe(II)/Lysine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the Complex Fe(II)/Alpha-Ketoglutarate Dependent Dioxygenase KDO1 with Fe(II)/Lysine within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl406 b:70.9 occ:1.00 CG1 A:VAL336 3.4 29.1 1.0 O A:HOH509 3.5 50.9 1.0 O A:LEU186 3.5 29.7 1.0 CD2 A:LEU186 3.9 37.5 1.0 NH1 A:ARG341 3.9 52.1 1.0 C A:LEU186 4.0 30.6 1.0 CA A:LEU186 4.1 30.1 1.0 CB A:VAL336 4.1 31.2 1.0 O A:ARG187 4.1 31.2 1.0 CB A:LEU186 4.4 30.8 1.0 CB A:ARG341 4.5 41.9 1.0 CB A:SER342 4.5 34.9 1.0 CG2 A:VAL336 4.6 31.1 1.0 CD1 A:ILE142 4.6 50.9 1.0 O A:HOH512 4.6 42.0 1.0 OH A:TYR144 4.7 30.6 1.0 O A:ASP338 4.7 44.1 1.0 CG A:LEU186 4.8 35.7 1.0 C A:ARG187 4.9 30.0 1.0 N A:SER342 4.9 34.9 1.0 N A:ARG187 5.0 26.8 1.0

K.Bastard, T.Isabet, E.A.Stura, P.Legrand, A.Zaparucha. Structural Studies Based on Two Lysine Dioxygenases with Distinct Regioselectivity Brings Insights Into Enzyme Specificity Within the Clavaminate Synthase-Like Family. Sci Rep V. 8 16587 2018.
ISSN: ESSN 2045-2322
PubMed: 30410048
DOI: 10.1038/S41598-018-34795-9