Magnesium in PDB 7euk: Crystal Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase in Complex with L-Orn

Enzymatic activity of Crystal Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase in Complex with L-Orn

All present enzymatic activity of Crystal Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase in Complex with L-Orn:
3.5.3.25;

Protein crystallography data

The structure of Crystal Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase in Complex with L-Orn, PDB code: 7euk was solved by K.Oda, Y.Matoba, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	44.00 / 1.40
*Space group*	P 1
*Cell size a, b, c (Å), α, β, γ (°)*	46.392, 46.963, 59.317, 83.53, 84.71, 70.14
*R / R_free (%)*	15.8 / 17.9

Other elements in 7euk:

The structure of Crystal Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase in Complex with L-Orn also contains other interesting chemical elements:

Manganese

(Mn)

4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase in Complex with L-Orn (pdb code 7euk). 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 Crystal Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase in Complex with L-Orn, PDB code: 7euk:

Magnesium binding site 1 out of 1 in 7euk

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Magnesium Binding Sites List in 7euk

Magnesium binding site 1 out of 1 in the Crystal Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase in Complex with L-Orn

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase in Complex with L-Orn within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg403 b:27.5 occ:1.00	O	A:HOH754	2.0	27.3	1.0
	O	A:HOH676	2.1	21.0	1.0
	O	A:ASN77	2.1	19.4	1.0
	O	A:HOH712	2.1	29.1	1.0
	O	A:HOH529	2.1	25.8	1.0
	O	A:HOH523	2.3	21.0	1.0
	C	A:ASN77	3.1	17.8	1.0
	O	A:ILE235	3.7	12.4	1.0
	N	A:ASN77	3.9	21.8	1.0
	N	A:LEU78	3.9	15.8	1.0
	O	A:HOH519	3.9	30.3	1.0
	CA	A:LEU78	4.1	13.1	1.0
	CA	A:ASN77	4.1	20.4	1.0
	O	A:HOH741	4.1	28.0	1.0
	C	A:ASP76	4.2	27.2	1.0
	O	A:GLY75	4.4	25.7	1.0
	O	A:ASP76	4.4	29.8	1.0
	C	A:ILE235	4.6	10.8	1.0
	N	A:THR79	4.6	11.4	1.0
	O	A:SER72	4.6	19.3	1.0
	OG1	A:THR79	4.7	13.6	1.0
	CA	A:ILE235	4.7	10.8	1.0
	O	A:LEU234	4.8	14.3	1.0
	C	A:LEU78	4.8	13.1	1.0
	O	A:HOH662	4.8	26.9	1.0
	CA	A:ASP76	4.9	28.3	1.0
	O	A:ILE73	4.9	24.7	1.0

Reference:

K.Oda, T.Sakaguchi, Y.Matoba. Catalytic Mechanism of Dcsb: Arginase Framework Used For Hydrolyzing Its Inhibitor. Protein Sci. V. 31 E4338 2022.
ISSN: ESSN 1469-896X
PubMed: 35634777
DOI: 10.1002/PRO.4338

Page generated: Wed Oct 2 20:59:08 2024

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