Atomistry » Magnesium » PDB 5cr7-5d2j » 5d2g
Atomistry »
  Magnesium »
    PDB 5cr7-5d2j »
      5d2g »

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: Sun Sep 29 02:27:53 2024

Last articles

Cl in 2WYT
Cl in 2WZC
Cl in 2WUV
Cl in 2WZB
Cl in 2WYJ
Cl in 2WYG
Cl in 2WVO
Cl in 2WXF
Cl in 2WWP
Cl in 2WW5
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy