Magnesium in PDB 1vj5: Human Soluble Epoxide Hydrolase- N-Cyclohexyl-N'-(4-Iodophenyl)Urea Complex

Enzymatic activity of Human Soluble Epoxide Hydrolase- N-Cyclohexyl-N'-(4-Iodophenyl)Urea Complex

All present enzymatic activity of Human Soluble Epoxide Hydrolase- N-Cyclohexyl-N'-(4-Iodophenyl)Urea Complex:
3.3.2.3;

Protein crystallography data

The structure of Human Soluble Epoxide Hydrolase- N-Cyclohexyl-N'-(4-Iodophenyl)Urea Complex, PDB code: 1vj5 was solved by G.A.Gomez, C.Morisseau, B.D.Hammock, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	48.94 / 2.35
*Space group*	P 6₅ 2 2
*Cell size a, b, c (Å), α, β, γ (°)*	93.510, 93.510, 245.700, 90.00, 90.00, 120.00
*R / R_free (%)*	21.7 / 26.6

Other elements in 1vj5:

The structure of Human Soluble Epoxide Hydrolase- N-Cyclohexyl-N'-(4-Iodophenyl)Urea Complex also contains other interesting chemical elements:

Iodine

(I)

1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Human Soluble Epoxide Hydrolase- N-Cyclohexyl-N'-(4-Iodophenyl)Urea Complex (pdb code 1vj5). 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 Human Soluble Epoxide Hydrolase- N-Cyclohexyl-N'-(4-Iodophenyl)Urea Complex, PDB code: 1vj5:

Magnesium binding site 1 out of 1 in 1vj5

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Magnesium Binding Sites List in 1vj5

Magnesium binding site 1 out of 1 in the Human Soluble Epoxide Hydrolase- N-Cyclohexyl-N'-(4-Iodophenyl)Urea Complex

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Soluble Epoxide Hydrolase- N-Cyclohexyl-N'-(4-Iodophenyl)Urea Complex within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg782 b:25.8 occ:1.00	OD2	A:ASP9	2.1	27.3	1.0
	O1	A:PO4783	2.3	60.5	1.0
	O	A:HOH1012	2.4	47.8	1.0
	O	A:ASP11	2.4	31.0	1.0
	OD1	A:ASP185	2.4	30.9	1.0
	O	A:HOH903	2.4	42.3	1.0
	CG	A:ASP9	3.1	27.2	1.0
	CG	A:ASP185	3.4	31.6	1.0
	C	A:ASP11	3.4	31.4	1.0
	OD1	A:ASP9	3.5	25.7	1.0
	P	A:PO4783	3.6	60.2	1.0
	OD2	A:ASP185	3.8	32.7	1.0
	CB	A:ASP11	3.8	32.9	1.0
	CA	A:ASP11	4.0	31.2	1.0
	O3	A:PO4783	4.0	59.9	1.0
	OD1	A:ASP184	4.0	30.5	1.0
	O2	A:PO4783	4.2	59.3	1.0
	N	A:ASP11	4.3	30.0	1.0
	CB	A:ASP9	4.4	27.1	1.0
	N	A:GLY12	4.4	30.8	1.0
	OD2	A:ASP11	4.6	35.5	1.0
	CD1	A:ILE186	4.6	40.4	1.0
	N	A:ASP185	4.6	31.0	1.0
	CB	A:ASP185	4.6	31.2	1.0
	O4	A:PO4783	4.7	59.8	1.0
	CG1	A:ILE186	4.7	37.5	1.0
	CG	A:ASP11	4.7	34.6	1.0
	CA	A:GLY12	4.7	30.1	1.0
	CG	A:ASP184	4.8	30.7	1.0
	OD2	A:ASP184	4.9	29.8	1.0

Reference:

G.A.Gomez, C.Morisseau, B.D.Hammock, D.W.Christianson. Structure of Human Epoxide Hydrolase Reveals Mechanistic Inferences on Bifunctional Catalysis in Epoxide and Phosphate Ester Hydrolysis Biochemistry V. 43 4716 2004.
ISSN: ISSN 0006-2960
PubMed: 15096040
DOI: 10.1021/BI036189J

Page generated: Sun Aug 10 05:16:48 2025

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