Chlorine in PDB 5d2h: 4-Oxalocrotonate Decarboxylase From Pseudomonas Putida G7 - Complexed with Magnesium and Alpha-Ketoglutarate

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

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

Protein crystallography data

The structure of 4-Oxalocrotonate Decarboxylase From Pseudomonas Putida G7 - Complexed with Magnesium and Alpha-Ketoglutarate, PDB code: 5d2h 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)*	42.27 / 1.94
*Space group*	P 2₁ 2₁ 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	43.741, 44.904, 125.318, 90.00, 90.00, 90.00
*R / R_free (%)*	16.3 / 23.1

Other elements in 5d2h:

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

Magnesium

(Mg)

1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the 4-Oxalocrotonate Decarboxylase From Pseudomonas Putida G7 - Complexed with Magnesium and Alpha-Ketoglutarate (pdb code 5d2h). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the 4-Oxalocrotonate Decarboxylase From Pseudomonas Putida G7 - Complexed with Magnesium and Alpha-Ketoglutarate, PDB code: 5d2h:

Chlorine binding site 1 out of 1 in 5d2h

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Chlorine Binding Sites List in 5d2h

Chlorine binding site 1 out of 1 in the 4-Oxalocrotonate Decarboxylase From Pseudomonas Putida G7 - Complexed with Magnesium and Alpha-Ketoglutarate

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of 4-Oxalocrotonate Decarboxylase From Pseudomonas Putida G7 - Complexed with Magnesium and Alpha-Ketoglutarate within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl312 b:26.2 occ:1.00	O	A:HOH458	3.0	26.8	1.0
	NE	A:ARG167	3.1	19.7	1.0
	N	A:ASP99	3.2	16.1	1.0
	NH2	A:ARG167	3.4	16.9	1.0
	CZ	A:ARG167	3.7	17.7	1.0
	CB	A:ASP99	3.8	15.7	1.0
	CA	A:ASP99	4.0	16.2	1.0
	O	A:HOH551	4.0	31.1	1.0
	O	A:ASP99	4.1	14.7	1.0
	CA	A:VAL98	4.1	16.9	1.0
	C	A:VAL98	4.2	15.8	1.0
	CD	A:LYS102	4.2	28.0	1.0
	CG1	A:VAL98	4.2	13.4	1.0
	CD	A:ARG167	4.3	16.0	1.0
	C	A:ASP99	4.5	18.3	1.0
	O	A:VAL97	4.6	15.4	1.0
	O	A:HOH473	4.7	21.0	1.0
	CB	A:LYS102	4.8	16.2	1.0
	CB	A:VAL98	4.8	17.2	1.0
	CG	A:LYS102	4.9	15.7	1.0

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: Sat Dec 12 11:37:44 2020

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