Chlorine in PDB 8qzb: D-2-Hydroxyacid Dehydrogenase (D2HDH) From Haloferax Mediterranei in Complex with 2-Ketohexanoic Acid, Nad+ and Chloride (1.16 A Resolution)

The structure of D-2-Hydroxyacid Dehydrogenase (D2HDH) From Haloferax Mediterranei in Complex with 2-Ketohexanoic Acid, Nad+ and Chloride (1.16 A Resolution), PDB code: 8qzb was solved by P.J.Baker, J.R.Barrett, A.A.A.B.Dakhil, J.Domenech, C.Bisson, N.Pramanpol, J.Ferrer, D.W.Rice, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.63 / 1.16
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	66.182, 74.777, 78.172, 109.07, 107.88, 95.56
R / Rfree (%)	13.5 / 16.5

The structure of D-2-Hydroxyacid Dehydrogenase (D2HDH) From Haloferax Mediterranei in Complex with 2-Ketohexanoic Acid, Nad+ and Chloride (1.16 A Resolution) also contains other interesting chemical elements:

Sodium	(Na)	12 atoms
Magnesium	(Mg)	19 atoms

The binding sites of Chlorine atom in the D-2-Hydroxyacid Dehydrogenase (D2HDH) From Haloferax Mediterranei in Complex with 2-Ketohexanoic Acid, Nad+ and Chloride (1.16 A Resolution) (pdb code 8qzb). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the D-2-Hydroxyacid Dehydrogenase (D2HDH) From Haloferax Mediterranei in Complex with 2-Ketohexanoic Acid, Nad+ and Chloride (1.16 A Resolution), PDB code: 8qzb:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the D-2-Hydroxyacid Dehydrogenase (D2HDH) From Haloferax Mediterranei in Complex with 2-Ketohexanoic Acid, Nad+ and Chloride (1.16 A Resolution)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of D-2-Hydroxyacid Dehydrogenase (D2HDH) From Haloferax Mediterranei in Complex with 2-Ketohexanoic Acid, Nad+ and Chloride (1.16 A Resolution) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl412 b:34.9 occ:1.00 OG A:SER167 3.2 18.8 1.0 N A:SER167 3.4 18.0 1.0 O A:HOH519 3.4 30.4 1.0 CB A:SER167 3.6 18.7 1.0 CD A:ARG165 3.7 19.9 1.0 O2B A:NAD401 3.8 31.9 1.0 NH1 A:ARG165 3.8 24.2 1.0 CG A:ARG165 3.8 16.9 1.0 N A:ARG166 3.8 18.4 1.0 NE A:ARG165 4.1 21.1 1.0 CB A:ARG165 4.1 17.1 1.0 CA A:SER167 4.1 18.2 1.0 CZ A:ARG165 4.3 22.1 1.0 C A:ARG166 4.3 19.6 1.0 CA A:ARG166 4.3 21.8 1.0 CB A:ARG166 4.3 25.0 1.0 C A:ARG165 4.5 15.7 1.0 CA A:ARG165 4.8 14.4 1.0 O3B A:NAD401 4.9 23.6 1.0

Chlorine binding site 2 out of 4 in the D-2-Hydroxyacid Dehydrogenase (D2HDH) From Haloferax Mediterranei in Complex with 2-Ketohexanoic Acid, Nad+ and Chloride (1.16 A Resolution)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of D-2-Hydroxyacid Dehydrogenase (D2HDH) From Haloferax Mediterranei in Complex with 2-Ketohexanoic Acid, Nad+ and Chloride (1.16 A Resolution) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl413 b:14.8 occ:1.00 NH1 B:ARG165 3.2 13.4 1.0 O B:HOH621 3.2 15.4 1.0 N B:SER167 3.2 12.5 1.0 OG B:SER167 3.3 13.4 1.0 O2B B:NAD401 3.4 11.7 1.0 O B:HOH660 3.5 23.4 1.0 N B:ARG166 3.6 11.1 1.0 CB B:SER167 3.6 13.7 1.0 CG B:ARG165 3.7 9.5 1.0 CD B:ARG165 3.8 10.5 1.0 CB B:ARG166 3.9 15.9 1.0 CB B:ARG165 4.0 9.4 1.0 CA B:SER167 4.0 11.8 1.0 CA B:ARG166 4.1 13.3 1.0 CZ B:ARG165 4.1 11.2 1.0 C B:ARG166 4.1 13.4 1.0 NE B:ARG165 4.2 11.6 1.0 C B:ARG165 4.3 10.7 1.0 CG B:ARG166 4.8 19.2 1.0 C2B B:NAD401 4.8 10.8 1.0 CA B:ARG165 4.8 9.7 1.0 O B:HOH853 4.9 24.4 1.0 O3B B:NAD401 4.9 11.2 1.0

Chlorine binding site 3 out of 4 in the D-2-Hydroxyacid Dehydrogenase (D2HDH) From Haloferax Mediterranei in Complex with 2-Ketohexanoic Acid, Nad+ and Chloride (1.16 A Resolution)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of D-2-Hydroxyacid Dehydrogenase (D2HDH) From Haloferax Mediterranei in Complex with 2-Ketohexanoic Acid, Nad+ and Chloride (1.16 A Resolution) within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl413 b:19.4 occ:1.00 O C:HOH581 3.2 32.3 1.0 OG C:SER167 3.2 15.9 1.0 N C:SER167 3.2 15.2 1.0 O C:HOH562 3.3 19.9 1.0 O C:HOH855 3.3 34.1 1.0 CB C:SER167 3.6 16.3 1.0 O2B C:NAD401 3.6 15.1 1.0 CD C:ARG165 3.6 15.9 1.0 NH1 C:ARG165 3.7 24.1 1.0 N C:ARG166 3.7 14.6 1.0 CG C:ARG165 3.7 12.4 1.0 CA C:SER167 4.0 15.5 1.0 NE C:ARG165 4.0 14.4 1.0 CB C:ARG166 4.0 17.8 1.0 CB C:ARG165 4.1 12.8 1.0 CA C:ARG166 4.2 14.8 1.0 C C:ARG166 4.2 15.9 1.0 CZ C:ARG165 4.2 17.4 1.0 C C:ARG165 4.4 14.9 1.0 O C:HOH577 4.7 50.8 1.0 CA C:ARG165 4.9 13.5 1.0 C2B C:NAD401 4.9 14.5 1.0 CG C:ARG166 4.9 21.0 1.0 O3B C:NAD401 5.0 14.3 1.0 O C:HOH823 5.0 30.2 1.0 N C:GLY168 5.0 14.5 1.0

Chlorine binding site 4 out of 4 in the D-2-Hydroxyacid Dehydrogenase (D2HDH) From Haloferax Mediterranei in Complex with 2-Ketohexanoic Acid, Nad+ and Chloride (1.16 A Resolution)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of D-2-Hydroxyacid Dehydrogenase (D2HDH) From Haloferax Mediterranei in Complex with 2-Ketohexanoic Acid, Nad+ and Chloride (1.16 A Resolution) within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl409 b:17.5 occ:1.00 O D:HOH600 3.2 18.0 1.0 N D:SER167 3.2 15.4 1.0 OG D:SER167 3.2 14.9 1.0 NH1 D:ARG165 3.3 17.9 1.0 O2B D:NAD401 3.4 12.0 1.0 O D:HOH576 3.5 25.6 1.0 N D:ARG166 3.5 12.2 1.0 CB D:SER167 3.6 17.1 1.0 CG D:ARG165 3.7 12.0 1.0 CD D:ARG165 3.7 13.7 1.0 CB D:ARG166 3.8 14.8 1.0 CA D:ARG166 3.9 13.6 1.0 CA D:SER167 4.0 15.6 1.0 CB D:ARG165 4.0 11.2 1.0 C D:ARG166 4.0 14.4 1.0 CZ D:ARG165 4.1 14.8 1.0 NE D:ARG165 4.2 13.0 1.0 C D:ARG165 4.3 12.3 1.0 C2B D:NAD401 4.7 11.1 1.0 CA D:ARG165 4.8 10.8 1.0 CG D:ARG166 4.8 19.7 1.0 O D:HOH782 4.9 50.5 1.0 O3B D:NAD401 4.9 11.4 1.0 O D:HOH813 4.9 39.1 1.0

J.Domenech, N.Pramanpol, C.Bisson, S.E.Sedelnikova, J.R.Barrett, A.A.A.B.Dakhil, A.S.Abdelhameed, S.E.Harding, D.W.Rice, P.J.Baker, J.Ferrer. Ternary Complexes of Haloferax Mediterranei D-2-Hydroxyacid Dehydrogenase Provide Insights Into Halophilicity and the Chiral Specificity of Its Reaction Mechanism. To Be Published.