Magnesium in PDB 2q0c: Terminal Uridylyl Transferase 4 From Trypanosoma Brucei with Bound Ctp

All present enzymatic activity of Terminal Uridylyl Transferase 4 From Trypanosoma Brucei with Bound Ctp:
2.7.7.52;

The structure of Terminal Uridylyl Transferase 4 From Trypanosoma Brucei with Bound Ctp, PDB code: 2q0c was solved by J.Stagno, H.Luecke, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.88 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	81.166, 42.157, 106.809, 90.00, 93.66, 90.00
R / Rfree (%)	23.2 / 28.1

The binding sites of Magnesium atom in the Terminal Uridylyl Transferase 4 From Trypanosoma Brucei with Bound Ctp (pdb code 2q0c). 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 Terminal Uridylyl Transferase 4 From Trypanosoma Brucei with Bound Ctp, PDB code: 2q0c:

Magnesium binding site 1 out of 1 in the Terminal Uridylyl Transferase 4 From Trypanosoma Brucei with Bound Ctp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Terminal Uridylyl Transferase 4 From Trypanosoma Brucei with Bound Ctp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:15.1 occ:1.00 O3G A:CTP501 2.3 26.2 1.0 O A:HOH544 2.4 22.6 1.0 O1B A:CTP501 2.5 28.9 1.0 OD2 A:ASP68 2.5 19.5 1.0 OD2 A:ASP66 2.5 33.0 1.0 O A:HOH595 2.6 21.6 1.0 O1A A:CTP501 2.6 31.5 1.0 PB A:CTP501 3.6 32.2 1.0 CG A:ASP66 3.6 32.3 1.0 CG A:ASP68 3.7 21.9 1.0 O A:HOH561 3.7 33.2 1.0 PA A:CTP501 3.8 29.8 1.0 PG A:CTP501 3.8 27.6 1.0 C5' A:CTP501 3.9 26.4 1.0 OD1 A:ASP66 4.0 32.1 1.0 O3A A:CTP501 4.0 31.3 1.0 O3B A:CTP501 4.0 29.8 1.0 OD1 A:ASP68 4.2 22.7 1.0 O A:HOH610 4.3 48.3 1.0 O5' A:CTP501 4.3 31.7 1.0 O A:ASP66 4.5 28.8 1.0 O A:HOH645 4.7 31.4 1.0 O1G A:CTP501 4.7 25.2 1.0 O A:HOH532 4.8 17.2 1.0 N A:SER54 4.8 20.1 1.0 OG A:SER54 4.8 21.9 1.0 O2G A:CTP501 4.8 30.9 1.0 C A:ASP66 4.8 29.1 1.0 CB A:ASP68 4.9 21.0 1.0 CA A:GLY53 4.9 18.0 1.0 O2B A:CTP501 5.0 26.5 1.0 CB A:ASP66 5.0 31.2 1.0

J.Stagno, I.Aphasizheva, R.Aphasizhev, H.Luecke. Dual Role of the Rna Substrate in Selectivity and Catalysis By Terminal Uridylyl Transferases. Proc.Natl.Acad.Sci.Usa V. 104 14634 2007.
ISSN: ISSN 0027-8424
PubMed: 17785418
DOI: 10.1073/PNAS.0704259104