Magnesium in PDB 3kna: M296I Mutant of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna

Enzymatic activity of M296I Mutant of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna

All present enzymatic activity of M296I Mutant of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna:
2.7.7.48;

Protein crystallography data

The structure of M296I Mutant of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna, PDB code: 3kna was solved by C.Ferrer-Orta, N.Verdaguer, R.Perez-Luque, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	74.00 / 2.80
*Space group*	P 4₁ 2₁ 2
*Cell size a, b, c (Å), α, β, γ (°)*	93.565, 93.565, 120.931, 90.00, 90.00, 90.00
*R / R_free (%)*	23.9 / 28

Magnesium Binding Sites:

The binding sites of Magnesium atom in the M296I Mutant of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna (pdb code 3kna). 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 M296I Mutant of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna, PDB code: 3kna:

Magnesium binding site 1 out of 1 in 3kna

Go back to

Magnesium Binding Sites List in 3kna

Magnesium binding site 1 out of 1 in the M296I Mutant of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of M296I Mutant of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg1055 b:74.2 occ:1.00	OD2	A:ASP238	2.4	53.5	1.0
	OD2	A:ASP240	3.0	54.5	1.0
	OD1	A:ASP339	3.1	50.4	1.0
	O	A:THR384	3.3	53.6	1.0
	CG	A:ASP238	3.4	54.2	1.0
	O	A:VAL239	3.7	53.1	1.0
	OD1	A:ASP238	3.7	54.4	1.0
	O	A:ILE340	4.1	51.6	1.0
	CG	A:ASP240	4.2	55.3	1.0
	CG	A:ASP339	4.4	49.7	1.0
	C	A:THR384	4.4	53.6	1.0
	CB	A:ALA367	4.5	67.3	1.0
	C	A:VAL239	4.5	54.2	1.0
	N	A:ILE340	4.7	50.1	1.0
	C	A:ASP238	4.7	55.0	1.0
	CB	A:ASP238	4.7	55.1	1.0
	OD1	A:ASP240	4.8	56.0	1.0
	N	A:VAL239	4.8	54.3	1.0
	CA	A:ASP238	4.9	54.7	1.0
	O	A:ASP238	5.0	56.0	1.0

Reference:

C.Ferrer-Orta, M.Sierra, R.Agudo, I.De La Higuera, A.Arias, R.Perez-Luque, C.Escarmis, E.Domingo, N.Verdaguer. Structure of Foot-and-Mouth Disease Virus Mutant Polymerases with Reduced Sensitivity to Ribavirin J.Virol. V. 84 6188 2010.
ISSN: ISSN 0022-538X
PubMed: 20392853
DOI: 10.1128/JVI.02420-09

Page generated: Wed Aug 14 18:11:22 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1

	© Copyright 2008-2020 by atomistry.com
Home \| Site Map \| Copyright \| Contact us \| Privacy