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: Sat Aug 21 16:44:19 2021

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy