Magnesium in PDB 4gw0: Crystal Structure of Arginine Kinase in Complex with Imino-L- Ornithine, Mgadp, and Nitrate.

Enzymatic activity of Crystal Structure of Arginine Kinase in Complex with Imino-L- Ornithine, Mgadp, and Nitrate.

All present enzymatic activity of Crystal Structure of Arginine Kinase in Complex with Imino-L- Ornithine, Mgadp, and Nitrate.:
2.7.3.3;

Protein crystallography data

The structure of Crystal Structure of Arginine Kinase in Complex with Imino-L- Ornithine, Mgadp, and Nitrate., PDB code: 4gw0 was solved by S.A.Clark, O.Davulcu, M.S.Chapman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	32.48 / 2.45
*Space group*	P 2₁ 2₁ 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	65.184, 71.103, 79.962, 90.00, 90.00, 90.00
*R / R_free (%)*	17.8 / 21

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Arginine Kinase in Complex with Imino-L- Ornithine, Mgadp, and Nitrate. (pdb code 4gw0). 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 Arginine Kinase in Complex with Imino-L- Ornithine, Mgadp, and Nitrate., PDB code: 4gw0:

Magnesium binding site 1 out of 1 in 4gw0

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Magnesium Binding Sites List in 4gw0

Magnesium binding site 1 out of 1 in the Crystal Structure of Arginine Kinase in Complex with Imino-L- Ornithine, Mgadp, and Nitrate.

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 Arginine Kinase in Complex with Imino-L- Ornithine, Mgadp, and Nitrate. within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg402 b:17.9 occ:1.00	O	A:HOH618	2.1	26.4	1.0
	O	A:HOH507	2.1	21.4	1.0
	O	A:HOH504	2.1	23.0	1.0
	O1	A:NO3404	2.2	18.3	0.9
	O1B	A:ADP401	2.3	14.0	0.9
	O1A	A:ADP401	2.4	17.7	0.9
	N	A:NO3404	3.1	18.4	0.9
	O3	A:NO3404	3.3	17.8	0.9
	PA	A:ADP401	3.5	18.6	0.9
	PB	A:ADP401	3.6	15.4	0.9
	O	A:HOH556	3.9	14.8	1.0
	CH1	A:ILO403	3.9	19.1	1.0
	O3A	A:ADP401	4.0	14.7	0.9
	O	A:HOH541	4.1	24.1	1.0
	OE2	A:GLU225	4.1	20.6	1.0
	OE2	A:GLU224	4.1	20.6	1.0
	OE2	A:GLU314	4.2	23.2	1.0
	NH1	A:ARG229	4.2	13.7	1.0
	O2	A:NO3404	4.3	18.4	0.9
	OE1	A:GLU224	4.4	20.4	1.0
	O3B	A:ADP401	4.4	13.4	0.9
	CZ3	A:TRP221	4.5	17.7	1.0
	O	A:HOH527	4.6	14.4	1.0
	O5'	A:ADP401	4.6	11.5	0.9
	O2B	A:ADP401	4.7	14.7	0.9
	O2A	A:ADP401	4.7	16.9	0.9
	CD	A:GLU224	4.7	20.1	1.0
	CD	A:GLU314	4.7	21.3	1.0
	C5'	A:ADP401	4.7	12.8	0.9
	NH2	A:ARG229	4.8	7.9	1.0
	CG	A:GLU314	4.9	21.0	1.0
	CH2	A:TRP221	4.9	17.8	1.0
	CZ	A:ARG229	5.0	11.2	1.0

Reference:

S.A.Clark, O.Davulcu, M.S.Chapman. Crystal Structures of Arginine Kinase in Complex with Adp, Nitrate, and Various Phosphagen Analogs. Biochem.Biophys.Res.Commun. V. 427 212 2012.
ISSN: ISSN 0006-291X
PubMed: 22995310
DOI: 10.1016/J.BBRC.2012.09.053

Page generated: Mon Aug 11 13:38:28 2025

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