Chlorine in PDB 8q3c: Structure of Selenomonas Ruminantium Lactate Dehydrogenase I85R Mutant

The structure of Structure of Selenomonas Ruminantium Lactate Dehydrogenase I85R Mutant, PDB code: 8q3c was solved by Q.Bertrand, S.Coquille, A.Iorio, F.Sterpone, D.Madern, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.81 / 3.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	72.29, 129.66, 133.41, 90, 90, 90
R / Rfree (%)	25.8 / 28.8

The binding sites of Chlorine atom in the Structure of Selenomonas Ruminantium Lactate Dehydrogenase I85R Mutant (pdb code 8q3c). 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 Selenomonas Ruminantium Lactate Dehydrogenase I85R Mutant, PDB code: 8q3c:

Chlorine binding site 1 out of 1 in the Structure of Selenomonas Ruminantium Lactate Dehydrogenase I85R Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Selenomonas Ruminantium Lactate Dehydrogenase I85R Mutant within 5.0Å range: probe atom residue distance (Å) B Occ N:Cl401 b:74.7 occ:1.00 HE N:ARG244 2.4 92.6 1.0 HG13 U:ILE56 2.4 96.5 1.0 HD21 N:LEU257 2.5 106.4 1.0 O U:HOH401 2.9 72.7 1.0 HG12 U:ILE56 3.0 96.5 1.0 HD22 N:LEU257 3.1 106.4 1.0 CG1 U:ILE56 3.1 79.3 1.0 NE N:ARG244 3.2 76.0 1.0 CD2 N:LEU257 3.2 87.5 1.0 HH21 N:ARG244 3.3 94.9 1.0 HE1 N:MET151 3.5 92.3 1.0 HB U:ILE56 3.5 85.3 1.0 HH22 N:ARG158 3.6 88.6 1.0 HD23 N:LEU257 3.6 106.4 1.0 HG21 N:THR255 3.8 101.8 1.0 HD3 N:ARG244 3.8 92.5 1.0 CB U:ILE56 3.9 70.0 1.0 NH2 N:ARG244 3.9 78.0 1.0 CZ N:ARG244 4.0 76.8 1.0 CD N:ARG244 4.0 75.9 1.0 HD11 N:LEU257 4.0 102.7 1.0 HG2 N:ARG244 4.0 93.3 1.0 HD11 U:ILE56 4.1 87.3 1.0 HG21 U:ILE56 4.2 85.6 1.0 NH2 N:ARG158 4.2 72.7 1.0 CD1 U:ILE56 4.3 71.7 1.0 CE N:MET151 4.4 75.8 1.0 HH21 N:ARG158 4.4 88.6 1.0 HE2 N:MET151 4.4 92.3 1.0 CG N:LEU257 4.4 86.5 1.0 HD13 N:LEU257 4.4 102.7 1.0 CG N:ARG244 4.5 76.7 1.0 CD1 N:LEU257 4.5 84.5 1.0 CG2 N:THR255 4.6 83.7 1.0 H U:ILE56 4.6 85.9 1.0 CG2 U:ILE56 4.6 70.2 1.0 HH22 N:ARG244 4.7 94.9 1.0 OD1 U:CSD55 4.7 75.1 1.0 HG3 N:ARG244 4.7 93.3 1.0 HG22 N:THR255 4.7 101.8 1.0 HD12 U:ILE56 4.7 87.3 1.0 HG23 N:THR255 4.8 101.8 1.0 HG N:LEU257 4.8 105.2 1.0 HD2 N:ARG244 4.9 92.5 1.0 HH12 N:ARG158 4.9 87.7 1.0 HE3 N:MET151 4.9 92.3 1.0 HD21 H:ASN171 4.9 101.2 1.0 HD13 U:ILE56 4.9 87.3 1.0 O2 N:NO3402 5.0 82.4 1.0

Q.Bertrand, S.Coquille, A.Iorio, F.Sterpone, D.Madern. Biochemical, Structural and Dynamical Characterizations of the Lactate Dehydrogenase From Selenomonas Ruminantium Provide Information About An Intermediate Evolutionary Step Prior to Complete Allosteric Regulation Acquisition in the Super Family of Lactate and Malate Dehydrogenases J.Struct.Biol. 2023.
ISSN: ESSN 1095-8657
DOI: 10.1016/J.JSB.2023.108039