Chlorine in PDB 8oe6: Structure of Hyperstable Haloalkane Dehalogenase Variant DHAA231

The structure of Structure of Hyperstable Haloalkane Dehalogenase Variant DHAA231, PDB code: 8oe6 was solved by M.Marek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.48 / 1.31
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	44.431, 67.998, 122.379, 90, 90, 90
R / Rfree (%)	15.4 / 16.8

The structure of Structure of Hyperstable Haloalkane Dehalogenase Variant DHAA231 also contains other interesting chemical elements:

Magnesium

(Mg)

4 atoms

The binding sites of Chlorine atom in the Structure of Hyperstable Haloalkane Dehalogenase Variant DHAA231 (pdb code 8oe6). 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 Structure of Hyperstable Haloalkane Dehalogenase Variant DHAA231, PDB code: 8oe6:

Chlorine binding site 1 out of 1 in the Structure of Hyperstable Haloalkane Dehalogenase Variant DHAA231


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Hyperstable Haloalkane Dehalogenase Variant DHAA231 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl305 b:20.9 occ:0.66 O A:HOH487 3.0 36.6 1.0 NE1 A:TRP107 3.2 19.0 1.0 N A:PRO206 3.4 22.4 1.0 ND2 A:ASN41 3.4 21.9 1.0 CA A:PRO206 3.5 22.7 1.0 CD A:PRO206 3.6 23.1 1.0 C A:PHE205 3.6 22.1 1.0 CD1 A:TRP107 3.7 18.4 1.0 CZ A:PHE168 3.7 21.9 1.0 CB A:PHE205 3.7 19.8 1.0 CB A:PRO206 3.8 23.1 1.0 O A:PHE205 3.9 21.7 1.0 CE2 A:PHE168 4.0 23.1 1.0 CB A:ASN41 4.0 18.3 1.0 CD1 A:LEU209 4.1 24.8 1.0 CG A:ASN41 4.2 18.8 1.0 CG A:LEU209 4.2 22.2 1.0 CA A:PHE205 4.3 20.1 1.0 CD2 A:LEU209 4.3 24.1 1.0 CG A:PRO206 4.3 23.1 1.0 CE2 A:TRP107 4.4 19.8 1.0 CE2 A:PHE149 4.5 23.9 1.0 CE1 A:PHE168 4.7 21.6 1.0 CG A:PHE205 4.8 19.9 1.0 O A:HOH664 4.9 38.1 1.0 OD2 A:ASP106 4.9 18.8 1.0 C A:PRO206 4.9 21.9 1.0

A.Kunka, S.M.Marques, M.Havlasek, M.Vasina, N.Velatova, L.Cengelova, D.Kovar, J.Damborsky, M.Marek, D.Bednar, Z.Prokop. Advancing Enzyme'S Stability and Catalytic Efficiency Through Synergy of Force-Field Calculations, Evolutionary Analysis, and Machine Learning. Acs Catalysis V. 13 12506 2023.
ISSN: ESSN 2155-5435
PubMed: 37822856
DOI: 10.1021/ACSCATAL.3C02575