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Magnesium in PDB 1ueu: 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: 1ueu 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) 48.40 / 2.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 86.835, 78.111, 77.815, 90.00, 97.65, 90.00
R / Rfree (%) 20.9 / 24.9

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 1ueu). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Divergent Evolutions of Trinucleotide Polymerization Revealed By An Archaeal Cca-Adding Enzyme Structure, PDB code: 1ueu:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1ueu

Go back to Magnesium Binding Sites List in 1ueu
Magnesium binding site 1 out of 2 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:Mg701

b:32.5
occ:1.00
OE2 A:GLU59 2.2 62.1 1.0
O3' A:CTP501 2.3 0.1 1.0
OD2 A:ASP61 2.4 42.0 1.0
O A:HOH854 2.6 54.2 1.0
OD2 A:ASP110 2.6 45.0 1.0
O A:HOH824 2.7 52.8 1.0
CG A:ASP61 3.3 45.5 1.0
C3' A:CTP501 3.5 0.7 1.0
CD A:GLU59 3.5 61.9 1.0
OD1 A:ASP61 3.6 46.2 1.0
CG A:ASP110 3.7 50.9 1.0
C4' A:CTP501 3.8 0.4 1.0
O A:HOH945 4.0 59.3 1.0
O2' A:CTP501 4.2 0.8 1.0
CB A:ASP110 4.3 42.9 1.0
C2' A:CTP501 4.3 0.9 1.0
OE1 A:GLU59 4.3 67.8 1.0
O4' A:CTP501 4.3 0.3 1.0
CG A:GLU59 4.4 57.8 1.0
C1' A:CTP501 4.4 0.0 1.0
MG A:MG702 4.5 64.3 1.0
CB A:ASP61 4.6 39.4 1.0
OD1 A:ASP110 4.7 47.1 1.0

Magnesium binding site 2 out of 2 in 1ueu

Go back to Magnesium Binding Sites List in 1ueu
Magnesium binding site 2 out of 2 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 2 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:Mg702

b:64.3
occ:1.00
O1B A:CTP501 2.4 0.2 1.0
O3' A:CTP501 2.5 0.1 1.0
C3' A:CTP501 2.7 0.7 1.0
OD1 A:ASP61 2.9 46.2 1.0
O A:HOH891 3.0 47.2 1.0
CG A:GLU59 3.2 57.8 1.0
O2' A:CTP501 3.3 0.8 1.0
CD A:GLU59 3.3 61.9 1.0
C2' A:CTP501 3.3 0.9 1.0
OE2 A:GLU59 3.4 62.1 1.0
O5' A:CTP501 3.4 0.2 1.0
N A:SER47 3.7 37.7 1.0
PB A:CTP501 3.9 0.2 1.0
O2A A:CTP501 3.9 0.1 1.0
CB A:SER47 3.9 35.9 1.0
OE1 A:GLU59 4.0 67.8 1.0
O A:GLU59 4.0 41.1 1.0
CG A:ASP61 4.0 45.5 1.0
C4' A:CTP501 4.1 0.4 1.0
PA A:CTP501 4.2 0.5 1.0
O3B A:CTP501 4.3 0.3 1.0
CA A:GLY46 4.4 42.1 1.0
OD2 A:ASP61 4.4 42.0 1.0
C5' A:CTP501 4.4 0.3 1.0
CA A:SER47 4.4 40.1 1.0
MG A:MG701 4.5 32.5 1.0
O3A A:CTP501 4.5 0.0 1.0
C A:GLY46 4.6 45.0 1.0
CB A:GLU59 4.6 45.1 1.0
N A:TYR48 4.7 39.4 1.0
C A:GLU59 4.7 42.2 1.0
C1' A:CTP501 4.8 0.0 1.0
O2B A:CTP501 5.0 0.1 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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