Magnesium in PDB 1uev: Divergent Evolutions of Trinucleotide Polymerization Revealed By An Archaeal Cca-Adding Enzyme Structure

Enzymatic activity of Divergent Evolutions of Trinucleotide Polymerization Revealed By An Archaeal Cca-Adding Enzyme Structure

All present enzymatic activity of Divergent Evolutions of Trinucleotide Polymerization Revealed By An Archaeal Cca-Adding Enzyme Structure:
2.7.7.25;

Protein crystallography data

The structure of Divergent Evolutions of Trinucleotide Polymerization Revealed By An Archaeal Cca-Adding Enzyme Structure, PDB code: 1uev was solved by O.Nureki, Riken Structural Genomics/Proteomics Initiative(Rsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	38.30 / 2.70
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	86.916, 77.742, 77.401, 90.00, 97.87, 90.00
*R / R_free (%)*	20.5 / 26

Other elements in 1uev:

The structure of Divergent Evolutions of Trinucleotide Polymerization Revealed By An Archaeal Cca-Adding Enzyme Structure also contains other interesting chemical elements:

Calcium

(Ca)

3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Divergent Evolutions of Trinucleotide Polymerization Revealed By An Archaeal Cca-Adding Enzyme Structure (pdb code 1uev). 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 Divergent Evolutions of Trinucleotide Polymerization Revealed By An Archaeal Cca-Adding Enzyme Structure, PDB code: 1uev:

Magnesium binding site 1 out of 1 in 1uev

Go back to

Magnesium Binding Sites List in 1uev

Magnesium binding site 1 out of 1 in the Divergent Evolutions of Trinucleotide Polymerization Revealed By An Archaeal Cca-Adding Enzyme Structure

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Divergent Evolutions of Trinucleotide Polymerization Revealed By An Archaeal Cca-Adding Enzyme Structure within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg601 b:48.6 occ:1.00	OE2	A:GLU59	2.4	58.4	1.0
	O	A:HOH687	2.5	46.5	1.0
	OD2	A:ASP110	2.6	60.5	1.0
	OD1	A:ASP61	2.6	42.3	1.0
	OD2	A:ASP61	3.0	51.2	1.0
	CG	A:ASP61	3.2	43.7	1.0
	CD	A:GLU59	3.5	58.0	1.0
	CG	A:ASP110	3.7	56.0	1.0
	O4'	A:ATP501	4.1	0.3	1.0
	OE1	A:GLU59	4.1	59.8	1.0
	C1'	A:ATP501	4.2	0.7	1.0
	CB	A:ASP110	4.2	48.0	1.0
	C4'	A:ATP501	4.3	0.9	1.0
	O3'	A:ATP501	4.3	0.1	1.0
	CG	A:GLU59	4.5	57.0	1.0
	CB	A:ASP61	4.6	39.8	1.0
	OD1	A:ASP110	4.6	54.0	1.0
	C8	A:ATP501	4.8	0.1	1.0
	C3'	A:ATP501	4.8	1.0	1.0
	N9	A:ATP501	5.0	0.6	1.0

Reference:

M.Okabe, K.Tomita, R.Ishitani, R.Ishii, N.Takeuchi, F.Arisaka, O.Nureki, S.Yokoyama. Divergent Evolutions of Trinucleotide Polymerization Revealed By An Archaeal Cca-Adding Enzyme Structure. Embo J. V. 22 5918 2003.
ISSN: ISSN 0261-4189
PubMed: 14592988
DOI: 10.1093/EMBOJ/CDG563

Page generated: Tue Aug 13 14:50:55 2024

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