Chlorine in PDB 5ugr: Malyl-Coa Lyase From Methylobacterium Extorquens

All present enzymatic activity of Malyl-Coa Lyase From Methylobacterium Extorquens:
4.1.3.24;

The structure of Malyl-Coa Lyase From Methylobacterium Extorquens, PDB code: 5ugr was solved by J.M.Gonzalez, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.44 / 1.56
Space group	P 6 2 2
Cell size a, b, c (Å), α, β, γ (°)	126.524, 126.524, 103.207, 90.00, 90.00, 120.00
R / Rfree (%)	10.2 / 13.4

The structure of Malyl-Coa Lyase From Methylobacterium Extorquens also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Chlorine atom in the Malyl-Coa Lyase From Methylobacterium Extorquens (pdb code 5ugr). 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 Malyl-Coa Lyase From Methylobacterium Extorquens, PDB code: 5ugr:

Chlorine binding site 1 out of 1 in the Malyl-Coa Lyase From Methylobacterium Extorquens


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Malyl-Coa Lyase From Methylobacterium Extorquens within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:17.5 occ:1.00 O A:HOH682 3.1 20.4 1.0 O A:HOH875 3.2 34.6 1.0 N A:ALA166 3.3 14.9 1.0 C A:GLY164 3.3 12.5 1.0 N A:ASP167 3.3 13.4 1.0 CA A:GLY164 3.5 12.8 1.0 O A:GLY164 3.5 13.5 1.0 N A:VAL165 3.6 12.8 1.0 CG A:PRO228 3.7 17.6 1.0 CB A:ALA166 3.7 21.0 1.0 CA A:ALA166 3.9 15.7 1.0 CD A:PRO228 4.0 14.6 1.0 C A:ALA166 4.1 13.2 1.0 CB A:ASP167 4.1 15.1 1.0 C A:VAL165 4.2 13.1 1.0 CA A:ASP167 4.3 12.9 1.0 CG A:ASP167 4.3 16.9 1.0 CA A:VAL165 4.5 13.1 1.0 OD2 A:ASP167 4.5 18.4 1.0 O A:HOH728 4.5 27.8 1.0 MG A:MG401 4.8 16.7 1.0 OE1 A:GLU140 4.8 18.6 1.0 OD1 A:ASP167 4.9 20.1 1.0 N A:GLY164 4.9 13.2 1.0

J.M.Gonzalez, R.Marti-Arbona, J.C.Chen, C.J.Unkefer. Structure of Methylobacterium Extorquens Malyl-Coa Lyase: Coa-Substrate Binding Correlates with Domain Shift. Acta Crystallogr F Struct V. 73 79 2017BIOL Commun.
ISSN: ESSN 2053-230X
PubMed: 28177317
DOI: 10.1107/S2053230X17001029