Magnesium in PDB 5fux: Catalytic Domain of Thymidine Kinase From Trypanosoma Brucei with Dtmp

Enzymatic activity of Catalytic Domain of Thymidine Kinase From Trypanosoma Brucei with Dtmp

All present enzymatic activity of Catalytic Domain of Thymidine Kinase From Trypanosoma Brucei with Dtmp:
2.7.1.21;

Protein crystallography data

The structure of Catalytic Domain of Thymidine Kinase From Trypanosoma Brucei with Dtmp, PDB code: 5fux was solved by J.Timm, M.Valente, V.Castillo-Acosta, T.Balzarini, J.E.Nettleship, H.Rada, K.S.Wilson, D.Gonzalez-Pacanowska, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	114.76 / 2.20
*Space group*	P 4₃ 2 2
*Cell size a, b, c (Å), α, β, γ (°)*	114.760, 114.760, 104.450, 90.00, 90.00, 90.00
*R / R_free (%)*	18.809 / 19.71

Other elements in 5fux:

The structure of Catalytic Domain of Thymidine Kinase From Trypanosoma Brucei with Dtmp also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Catalytic Domain of Thymidine Kinase From Trypanosoma Brucei with Dtmp (pdb code 5fux). 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 Catalytic Domain of Thymidine Kinase From Trypanosoma Brucei with Dtmp, PDB code: 5fux:

Magnesium binding site 1 out of 1 in 5fux

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Magnesium Binding Sites List in 5fux

Magnesium binding site 1 out of 1 in the Catalytic Domain of Thymidine Kinase From Trypanosoma Brucei with Dtmp

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Catalytic Domain of Thymidine Kinase From Trypanosoma Brucei with Dtmp within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg1385 b:65.5 occ:1.00	O2	A:PO41387	2.3	50.5	1.0
	O3P	A:QBT1388	2.4	58.9	0.5
	OG1	A:THR219	2.5	41.3	1.0
	O	A:HOH2008	2.5	77.3	1.0
	O	A:HOH2009	2.6	55.5	1.0
	P	A:QBT1388	3.1	65.0	0.5
	P	A:PO41387	3.4	49.1	1.0
	O3	A:PO41387	3.5	59.9	1.0
	O1P	A:QBT1388	3.5	31.3	0.5
	CB	A:THR219	3.6	42.8	1.0
	O2P	A:QBT1388	3.7	39.7	0.5
	N	A:THR219	3.9	36.1	1.0
	OD1	A:ASP285	4.1	52.6	1.0
	O4	A:PO41387	4.2	45.2	1.0
	CA	A:THR219	4.3	40.2	1.0
	CD	A:GLU286	4.4	70.3	1.0
	OE1	A:GLU286	4.4	74.6	1.0
	OE2	A:GLU286	4.4	65.9	1.0
	OG	A:SER310	4.4	50.7	1.0
	NZ	A:LYS218	4.6	39.6	1.0
	O1	A:PO41387	4.6	51.7	1.0
	O5'	A:QBT1388	4.6	69.0	1.0
	CE	A:LYS218	4.6	36.4	1.0
	O	A:HOH2007	4.7	43.0	1.0
	CB	A:LYS218	4.7	36.8	1.0
	CG2	A:THR219	4.8	40.6	1.0
	OD2	A:ASP285	4.8	61.6	1.0
	CG	A:ASP285	4.9	47.4	1.0
	C	A:LYS218	4.9	36.1	1.0
	CG	A:GLU286	5.0	56.1	1.0

Reference:

M.Valente, J.Timm, V.M.Castillo-Acosta, L.M.Ruiz-Perez, T.Balzarini, J.E.Nettleship, L.E.Bird, H.Rada, K.S.Wilson, D.Gonzalez-Pacanowska. Cell Cycle Regulation and Novel Structural Features of Thymidine Kinase, An Essential Enzyme in Trypanosoma Brucei. Mol.Microbiol. V. 102 365 2016.
ISSN: ISSN 0950-382X
PubMed: 27426054
DOI: 10.1111/MMI.13467

Page generated: Mon Dec 14 20:19:47 2020

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