Magnesium in PDB 7v1g: Crystal Structure of Omsk Hemorrhagic Fever Virus NS5 Mtase (with A Gmp-ARG28 Adduct and in Complex with Sam)

Enzymatic activity of Crystal Structure of Omsk Hemorrhagic Fever Virus NS5 Mtase (with A Gmp-ARG28 Adduct and in Complex with Sam)

All present enzymatic activity of Crystal Structure of Omsk Hemorrhagic Fever Virus NS5 Mtase (with A Gmp-ARG28 Adduct and in Complex with Sam):
3.4.21.91; 3.6.1.15; 3.6.4.13;

Protein crystallography data

The structure of Crystal Structure of Omsk Hemorrhagic Fever Virus NS5 Mtase (with A Gmp-ARG28 Adduct and in Complex with Sam), PDB code: 7v1g was solved by H.Jia, P.Gong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	32.71 / 1.38
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	35.125, 89.685, 45.452, 90, 90.47, 90
*R / R_free (%)*	20 / 22.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Omsk Hemorrhagic Fever Virus NS5 Mtase (with A Gmp-ARG28 Adduct and in Complex with Sam) (pdb code 7v1g). 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 Omsk Hemorrhagic Fever Virus NS5 Mtase (with A Gmp-ARG28 Adduct and in Complex with Sam), PDB code: 7v1g:

Magnesium binding site 1 out of 1 in 7v1g

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Magnesium Binding Sites List in 7v1g

Magnesium binding site 1 out of 1 in the Crystal Structure of Omsk Hemorrhagic Fever Virus NS5 Mtase (with A Gmp-ARG28 Adduct and in Complex with Sam)

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 Omsk Hemorrhagic Fever Virus NS5 Mtase (with A Gmp-ARG28 Adduct and in Complex with Sam) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg301 b:34.1 occ:1.00	O	A:HOH437	2.1	23.7	1.0
	OG	A:SER150	2.1	18.1	0.5
	O	A:HOH490	2.6	26.7	1.0
	O	A:HOH420	2.8	16.3	1.0
	OG1	A:THR217	2.9	14.0	1.0
	CB	A:THR217	3.2	11.1	1.0
	CD1	A:LEU185	3.4	12.8	1.0
	CB	A:SER150	3.5	17.4	0.5
	CB	A:SER150	3.5	17.4	0.5
	O1B	A:GTP305	3.8	27.9	0.6
	CA	A:SER150	4.2	12.9	0.5
	CA	A:SER150	4.2	12.9	0.5
	CG2	A:THR217	4.3	15.3	1.0
	CA	A:THR217	4.3	11.7	1.0
	O	A:HOH432	4.3	29.1	1.0
	O2B	A:GTP305	4.4	31.8	0.6
	PB	A:GTP305	4.4	32.6	0.6
	NZ	A:LYS183	4.5	21.0	1.0
	N	A:SER150	4.5	17.7	0.5
	N	A:SER150	4.5	17.7	0.5
	O	A:HOH486	4.5	13.1	1.0
	O3A	A:GTP305	4.6	32.3	0.6
	O	A:HOH401	4.6	30.1	1.0
	OE2	A:GLU157	4.6	16.4	1.0
	OE1	A:GLU219	4.6	17.7	1.0
	OG	A:SER150	4.7	17.0	0.5
	O	A:GLY148	4.8	15.2	1.0
	CG	A:LEU185	4.8	12.1	1.0
	O	A:HOH449	4.8	38.5	1.0
	CE	A:LYS183	4.9	20.8	1.0
	O	A:HOH428	4.9	18.2	1.0
	O	A:SER216	5.0	19.7	1.0

Reference:

H.Jia, Y.Zhong, C.Peng, P.Gong. Crystal Structures of Flavivirus NS5 Guanylyltransferase Reveal A Gmp-Arginine Adduct. J.Virol. V. 96 41822 2022.
ISSN: ESSN 1098-5514
PubMed: 35758665
DOI: 10.1128/JVI.00418-22

Page generated: Thu Aug 14 16:51:58 2025

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