Magnesium in PDB 7mgo: Crystal Structure of F501H Variant of 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase (2-Kpcc) From Xanthobacter Autotrophicus

All present enzymatic activity of Crystal Structure of F501H Variant of 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase (2-Kpcc) From Xanthobacter Autotrophicus:
1.8.1.5;

The structure of Crystal Structure of F501H Variant of 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase (2-Kpcc) From Xanthobacter Autotrophicus, PDB code: 7mgo was solved by G.Prussia, O.A.Zadvornyy, J.W.Peters, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.19 / 1.85
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	87.093, 60.209, 104.978, 90, 100.47, 90
R / Rfree (%)	17.2 / 20.3

The binding sites of Magnesium atom in the Crystal Structure of F501H Variant of 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase (2-Kpcc) From Xanthobacter Autotrophicus (pdb code 7mgo). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of F501H Variant of 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase (2-Kpcc) From Xanthobacter Autotrophicus, PDB code: 7mgo:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of F501H Variant of 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase (2-Kpcc) From Xanthobacter Autotrophicus


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of F501H Variant of 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase (2-Kpcc) From Xanthobacter Autotrophicus within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg603 b:31.2 occ:1.00 OG A:SER450 2.5 20.7 1.0 O A:VAL429 2.5 21.2 1.0 O A:LEU431 2.6 25.1 1.0 O A:ALA447 2.6 19.2 1.0 O A:HOH758 2.6 23.1 1.0 O A:LEU427 3.2 22.6 1.0 C A:LEU431 3.5 23.4 1.0 C A:ALA447 3.6 22.2 1.0 C A:VAL429 3.7 23.8 1.0 CB A:SER450 3.7 18.1 1.0 N A:LEU431 4.0 23.4 1.0 CD A:PRO432 4.1 21.5 1.0 N A:PRO432 4.1 21.3 1.0 CA A:HIS448 4.2 23.5 1.0 N A:SER450 4.2 19.0 1.0 N A:HIS448 4.3 23.5 1.0 N A:VAL429 4.3 27.3 1.0 CA A:LEU431 4.4 18.8 1.0 C A:LEU427 4.4 19.3 1.0 CA A:SER450 4.4 20.6 1.0 C A:ALA430 4.5 28.4 1.0 CG2 A:VAL429 4.5 22.6 1.0 C A:HIS448 4.5 28.6 1.0 CA A:ALA447 4.5 21.1 1.0 O A:PRO432 4.5 22.5 1.0 CB A:ALA447 4.6 22.2 1.0 N A:ALA430 4.6 28.0 1.0 CG A:PRO420 4.6 31.2 1.0 CA A:VAL429 4.6 24.1 1.0 O A:GLY451 4.6 21.8 1.0 CA A:ALA430 4.7 28.9 1.0 O A:HIS448 4.7 23.3 1.0 N A:GLY451 4.8 22.9 1.0 C A:SER450 4.8 21.3 1.0 CB A:PRO420 5.0 22.4 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of F501H Variant of 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase (2-Kpcc) From Xanthobacter Autotrophicus


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of F501H Variant of 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase (2-Kpcc) From Xanthobacter Autotrophicus within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg603 b:41.0 occ:1.00 O B:HOH927 2.3 36.8 1.0 OG B:SER450 2.5 30.3 1.0 O B:ALA447 2.6 28.9 1.0 O B:LEU431 2.6 33.2 1.0 O B:VAL429 2.6 31.1 1.0 O B:LEU427 3.0 38.2 1.0 C B:LEU431 3.5 26.3 1.0 C B:ALA447 3.5 39.3 1.0 CB B:SER450 3.7 26.6 1.0 C B:VAL429 3.8 31.2 1.0 N B:LEU431 4.1 34.6 1.0 CD B:PRO432 4.2 24.1 1.0 C B:LEU427 4.2 37.3 1.0 N B:PRO432 4.2 29.7 1.0 CA B:HIS448 4.2 28.0 1.0 N B:HIS448 4.2 29.5 1.0 N B:SER450 4.2 24.9 1.0 N B:VAL429 4.3 31.0 1.0 CA B:LEU431 4.4 33.5 1.0 CA B:SER450 4.4 25.9 1.0 CG B:PRO420 4.5 37.0 1.0 CG2 B:VAL429 4.5 32.1 1.0 C B:HIS448 4.5 39.6 1.0 CA B:ALA447 4.5 35.6 1.0 CB B:ALA447 4.6 29.7 1.0 O B:PRO432 4.6 30.3 1.0 O B:GLY451 4.6 27.5 1.0 C B:ALA430 4.6 41.7 1.0 O B:HIS448 4.7 27.5 1.0 CA B:VAL429 4.7 32.9 1.0 N B:ALA430 4.7 33.5 1.0 CA B:LEU427 4.8 42.1 1.0 C B:SER450 4.8 32.9 1.0 CB B:PRO420 4.8 27.6 1.0 N B:GLY451 4.8 25.1 1.0 CA B:ALA430 4.8 30.5 1.0

G.Prussia, K.Shisler, O.A.Zadvornyy, B.R.Streit, J.L.Dubois, J.W.Peters. The Unique Phe-His Dyad of 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase Selectively Promotes Carboxylation and S-C Bond Cleavage J.Biol.Chem. 2021.
ISSN: ESSN 1083-351X