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Magnesium in PDB 5d2g: 4-Oxalocrotonate Decarboxylase From Pseudomonas Putida G7 - Complexed with Magnesium

Enzymatic activity of 4-Oxalocrotonate Decarboxylase From Pseudomonas Putida G7 - Complexed with Magnesium

All present enzymatic activity of 4-Oxalocrotonate Decarboxylase From Pseudomonas Putida G7 - Complexed with Magnesium:
4.1.1.77;

Protein crystallography data

The structure of 4-Oxalocrotonate Decarboxylase From Pseudomonas Putida G7 - Complexed with Magnesium, PDB code: 5d2g was solved by S.L.Guimaraes, R.A.P.Nagem, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.45 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 42.766, 45.035, 124.666, 90.00, 90.00, 90.00
R / Rfree (%) 15.4 / 20.4

Other elements in 5d2g:

The structure of 4-Oxalocrotonate Decarboxylase From Pseudomonas Putida G7 - Complexed with Magnesium also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the 4-Oxalocrotonate Decarboxylase From Pseudomonas Putida G7 - Complexed with Magnesium (pdb code 5d2g). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the 4-Oxalocrotonate Decarboxylase From Pseudomonas Putida G7 - Complexed with Magnesium, PDB code: 5d2g:

Magnesium binding site 1 out of 1 in 5d2g

Go back to Magnesium Binding Sites List in 5d2g
Magnesium binding site 1 out of 1 in the 4-Oxalocrotonate Decarboxylase From Pseudomonas Putida G7 - Complexed with Magnesium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of 4-Oxalocrotonate Decarboxylase From Pseudomonas Putida G7 - Complexed with Magnesium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:9.2
occ:1.00
 OE1 A:GLU111 1.9 8.2 1.0
O A:HOH488 1.9 17.9 1.0
OE1 A:GLU142 1.9 11.2 1.0
OE2 A:GLU109 2.0 15.3 1.0
O A:HOH480 2.0 6.2 1.0
O A:HOH478 2.1 14.3 1.0
CD A:GLU111 2.9 10.9 1.0
CD A:GLU109 3.0 18.9 1.0
CD A:GLU142 3.2 10.4 1.0
OE2 A:GLU111 3.4 12.3 1.0
O A:MET65 3.7 10.1 1.0
OE1 A:GLU109 3.8 22.4 1.0
CB A:GLU142 3.8 9.3 1.0
CG A:GLU109 3.8 17.6 1.0
NZ A:LYS64 4.0 7.2 1.0
CG A:GLU142 4.1 8.3 1.0
OE2 A:GLU142 4.1 7.1 1.0
CE A:LYS64 4.1 14.7 1.0
O1 A:EDO302 4.2 40.4 1.0
CG A:GLU111 4.2 11.2 1.0
CG2 A:ILE144 4.3 8.6 1.0
N A:GLY236 4.7 12.8 1.0
CA A:GLY235 4.7 8.8 1.0
C A:GLY235 4.8 8.1 1.0
CE A:MET233 4.8 11.4 1.0
C A:MET65 4.9 13.5 1.0
O A:HOH551 4.9 6.2 0.5
O A:HOH551 4.9 6.2 0.5

Reference:

S.L.Guimaraes, J.B.Coitinho, D.M.Costa, S.S.Araujo, C.P.Whitman, R.A.Nagem. Crystal Structures of Apo and Liganded 4-Oxalocrotonate Decarboxylase Uncover A Structural Basis For the Metal-Assisted Decarboxylation of A Vinylogous Beta-Keto Acid. Biochemistry V. 55 2632 2016.
ISSN: ISSN 0006-2960
PubMed: 27082660
DOI: 10.1021/ACS.BIOCHEM.6B00050
Page generated: Mon Dec 14 20:09:48 2020

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