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 / R_free (%)*	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

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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

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