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Magnesium in PDB 7mgn: Crystal Structure of F501H/H506E Variant of 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase (2-Kpcc) From Xanthobacter Autotrophicus

Enzymatic activity of Crystal Structure of F501H/H506E Variant of 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase (2-Kpcc) From Xanthobacter Autotrophicus

All present enzymatic activity of Crystal Structure of F501H/H506E Variant of 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase (2-Kpcc) From Xanthobacter Autotrophicus:
1.8.1.5;

Protein crystallography data

The structure of Crystal Structure of F501H/H506E Variant of 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase (2-Kpcc) From Xanthobacter Autotrophicus, PDB code: 7mgn was solved by O.A.Zadvornyy, G.Prussia, J.W.Peters, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.66 / 1.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 87.006, 60.111, 105.14, 90, 100.52, 90
R / Rfree (%) 14.1 / 18.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of F501H/H506E Variant of 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase (2-Kpcc) From Xanthobacter Autotrophicus (pdb code 7mgn). 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/H506E Variant of 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase (2-Kpcc) From Xanthobacter Autotrophicus, PDB code: 7mgn:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 7mgn

Go back to Magnesium Binding Sites List in 7mgn
Magnesium binding site 1 out of 2 in the Crystal Structure of F501H/H506E 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/H506E 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:14.9
occ:0.78
 O A:HOH849 2.3 15.4 0.9
OG A:SER450 2.4 17.0 1.0
O A:VAL429 2.5 17.7 1.0
O A:ALA447 2.5 16.9 1.0
O A:LEU431 2.6 20.2 1.0
O A:LEU427 3.2 19.3 1.0
C A:LEU431 3.5 14.3 0.8
C A:ALA447 3.5 16.2 1.0
CB A:SER450 3.6 16.6 1.0
C A:VAL429 3.7 15.2 1.0
N A:LEU431 4.1 19.4 1.0
N A:PRO432 4.1 13.9 0.9
N A:SER450 4.1 14.8 1.0
CD A:PRO432 4.2 13.9 1.0
CA A:HIS448 4.2 16.6 1.0
N A:HIS448 4.2 14.6 1.0
N A:VAL429 4.3 21.9 1.0
CA A:SER450 4.3 16.4 1.0
CA A:LEU431 4.4 14.4 1.0
C A:LEU427 4.4 14.8 1.0
C A:HIS448 4.4 14.3 0.7
C A:ALA430 4.5 22.2 1.0
CA A:ALA447 4.5 16.3 1.0
O A:GLY451 4.5 13.8 0.9
CG2 A:VAL429 4.5 15.1 1.0
CB A:ALA447 4.6 16.9 1.0
N A:ALA430 4.6 18.6 1.0
CA A:VAL429 4.6 18.9 1.0
O A:PRO432 4.6 18.6 1.0
O A:HIS448 4.6 15.9 1.0
CG A:PRO420 4.7 22.3 0.9
N A:GLY451 4.7 21.4 1.0
CA A:ALA430 4.7 15.1 1.0
C A:SER450 4.7 15.9 0.9

Magnesium binding site 2 out of 2 in 7mgn

Go back to Magnesium Binding Sites List in 7mgn
Magnesium binding site 2 out of 2 in the Crystal Structure of F501H/H506E 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/H506E 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:20.1
occ:0.61
 O B:HOH958 2.2 23.7 1.0
OG B:SER450 2.4 24.2 1.0
O B:ALA447 2.5 21.4 1.0
O B:VAL429 2.6 26.4 1.0
O B:LEU431 2.7 22.6 1.0
O B:LEU427 3.1 26.6 1.0
C B:ALA447 3.5 21.2 0.9
C B:LEU431 3.6 17.6 0.8
CB B:SER450 3.6 22.2 1.0
C B:VAL429 3.8 19.8 0.8
N B:SER450 4.1 19.1 1.0
CD B:PRO432 4.2 19.2 1.0
N B:PRO432 4.2 17.1 0.8
N B:LEU431 4.2 27.8 1.0
CA B:HIS448 4.2 23.0 1.0
N B:HIS448 4.3 21.7 1.0
CA B:SER450 4.3 18.5 1.0
C B:LEU427 4.3 21.3 0.8
N B:VAL429 4.3 21.1 0.9
CA B:ALA447 4.4 21.9 0.9
C B:HIS448 4.4 21.0 0.8
CA B:LEU431 4.5 19.2 0.8
CG2 B:VAL429 4.5 20.9 1.0
CB B:ALA447 4.5 30.3 1.0
CG B:PRO420 4.6 30.7 0.9
O B:GLY451 4.6 22.2 1.0
O B:HIS448 4.6 21.9 1.0
C B:ALA430 4.6 20.0 0.7
O B:PRO432 4.6 20.5 0.8
CA B:VAL429 4.7 20.9 0.8
C B:SER450 4.7 20.6 0.8
N B:GLY451 4.7 21.9 1.0
N B:ALA430 4.7 24.8 0.9
CA B:ALA430 4.8 23.3 1.0
CA B:LEU427 4.9 26.1 0.9
N B:MET449 5.0 22.5 1.0

Reference:

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
Page generated: Thu Oct 3 00:51:16 2024

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