Magnesium in PDB 2dr8: Complex Structure of Cca-Adding Enzyme with Trnaminidc and Ctp

All present enzymatic activity of Complex Structure of Cca-Adding Enzyme with Trnaminidc and Ctp:
2.7.7.21; 2.7.7.25;

The structure of Complex Structure of Cca-Adding Enzyme with Trnaminidc and Ctp, PDB code: 2dr8 was solved by K.Tomita, R.Ishitani, S.Fukai, O.Nureki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	9.98 / 2.50
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	58.029, 58.029, 429.507, 90.00, 90.00, 90.00
R / Rfree (%)	22.4 / 25.7

The binding sites of Magnesium atom in the Complex Structure of Cca-Adding Enzyme with Trnaminidc and Ctp (pdb code 2dr8). 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 Complex Structure of Cca-Adding Enzyme with Trnaminidc and Ctp, PDB code: 2dr8:

Magnesium binding site 1 out of 1 in the Complex Structure of Cca-Adding Enzyme with Trnaminidc and Ctp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Complex Structure of Cca-Adding Enzyme with Trnaminidc and Ctp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg503 b:80.2 occ:1.00 OD1 A:ASP61 2.4 50.6 1.0 O3G A:CTP501 2.7 40.7 1.0 O2B A:CTP501 2.8 40.5 1.0 O1A A:CTP501 3.0 42.3 1.0 O A:GLU59 3.1 54.0 1.0 CG A:ASP61 3.2 50.6 1.0 OD2 A:ASP61 3.4 51.4 1.0 O A:HOH530 3.5 46.8 1.0 CG A:GLU59 3.8 57.9 1.0 OG A:SER47 3.9 44.0 1.0 CB A:GLU59 3.9 55.0 1.0 PB A:CTP501 3.9 38.1 1.0 O A:HOH615 3.9 56.8 1.0 C A:GLU59 4.0 53.0 1.0 CD A:GLU59 4.1 61.0 1.0 O3A A:CTP501 4.2 40.2 1.0 PA A:CTP501 4.2 42.4 1.0 PG A:CTP501 4.2 40.8 1.0 OE2 A:GLU59 4.4 59.8 1.0 O3B A:CTP501 4.4 38.9 1.0 OE1 A:GLU59 4.5 63.7 1.0 CA A:GLU59 4.5 53.8 1.0 O A:HOH594 4.6 40.0 1.0 CB A:ASP61 4.6 48.2 1.0 N A:SER47 4.8 43.1 1.0 O1G A:CTP501 4.9 41.0 1.0 N A:ASP61 5.0 47.9 1.0

K.Tomita, R.Ishitani, S.Fukai, O.Nureki. Complete Crystallographic Analysis of the Dynamics of Cca Sequence Addition Nature V. 443 956 2006.
ISSN: ISSN 0028-0836
PubMed: 17051158
DOI: 10.1038/NATURE05204