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 2P94
Cl in 2P95
Cl in 2P7H
Cl in 2P93
Cl in 2P67
Cl in 2P7I
Cl in 2P82
Cl in 2P7A
Cl in 2P6X
Cl in 2P5V
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy