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Calcium 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 / Rfree (%) 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:

Magnesium (Mg) 1 atom

Calcium Binding Sites:

The binding sites of Calcium 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 Calcium atom.
In total 3 binding sites of Calcium where determined in the Divergent Evolutions of Trinucleotide Polymerization Revealed By An Archaeal Cca-Adding Enzyme Structure, PDB code: 1uev:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in 1uev

Go back to Calcium Binding Sites List in 1uev
Calcium binding site 1 out of 3 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 Calcium with other atoms in the Ca 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:Ca602

b:71.1
occ:1.00
 O A:LYS166 2.8 24.8 1.0
CA A:CA604 3.6 77.1 1.0
C A:LYS166 4.0 26.8 1.0
O A:HOH614 4.0 25.6 1.0
CG A:LYS166 4.3 15.2 1.0
CA A:VAL167 4.5 26.7 1.0
O A:HOH629 4.7 27.8 1.0
N A:VAL167 4.7 29.8 1.0

Calcium binding site 2 out of 3 in 1uev

Go back to Calcium Binding Sites List in 1uev
Calcium binding site 2 out of 3 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 Calcium with other atoms in the Ca 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:Ca603

b:94.7
occ:1.00
 OE1 A:GLU387 3.0 60.4 1.0
OG1 A:THR383 3.3 23.6 1.0
OE2 A:GLU387 3.6 56.5 1.0
O A:HOH627 3.7 41.7 1.0
CD A:GLU387 3.7 51.8 1.0
O A:HOH690 4.7 40.7 1.0
CB A:THR383 4.8 21.0 1.0
CG2 A:THR384 4.8 24.0 1.0
OG1 A:THR384 5.0 27.7 1.0

Calcium binding site 3 out of 3 in 1uev

Go back to Calcium Binding Sites List in 1uev
Calcium binding site 3 out of 3 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 Calcium with other atoms in the Ca binding site number 3 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:Ca604

b:77.1
occ:1.00
 O A:HOH614 2.9 25.6 1.0
O A:HOH675 3.0 47.3 1.0
CA A:CA602 3.6 71.1 1.0
O A:GLY159 3.9 31.6 1.0
O A:HOH689 4.3 37.0 1.0
OD1 A:ASN234 4.4 30.6 1.0
O A:VAL167 4.5 29.2 1.0
C A:GLY159 4.9 27.1 1.0
ND2 A:ASN234 4.9 33.9 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 Jul 8 02:31:36 2025

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