Magnesium in PDB 5z4m: Structure of TAILORD343A with Bound Utp and Mg

All present enzymatic activity of Structure of TAILORD343A with Bound Utp and Mg:
2.7.7.52;

The structure of Structure of TAILORD343A with Bound Utp and Mg, PDB code: 5z4m was solved by L.Cheng, F.Li, Y.Jiang, H.Yu, C.Xie, Y.Shi, Q.Gong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.98 / 1.74
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	61.962, 84.556, 149.347, 90.00, 90.00, 90.00
R / Rfree (%)	16.7 / 20.6

The binding sites of Magnesium atom in the Structure of TAILORD343A with Bound Utp and Mg (pdb code 5z4m). 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 Structure of TAILORD343A with Bound Utp and Mg, PDB code: 5z4m:

Magnesium binding site 1 out of 1 in the Structure of TAILORD343A with Bound Utp and Mg


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of TAILORD343A with Bound Utp and Mg within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg603 b:26.5 occ:1.00 O1B A:UTP602 2.0 25.9 1.0 O2A A:UTP602 2.1 25.4 1.0 OD1 A:ASP278 2.1 26.5 1.0 OD2 A:ASP280 2.1 20.9 1.0 O A:HOH711 2.1 24.6 1.0 O1G A:UTP602 2.2 23.1 1.0 CG A:ASP280 3.1 26.2 1.0 H5'1 A:UTP602 3.1 30.0 1.0 CG A:ASP278 3.2 30.4 1.0 PB A:UTP602 3.2 27.4 1.0 PA A:UTP602 3.3 29.6 1.0 H A:SER267 3.4 24.0 1.0 OD1 A:ASP280 3.4 23.4 1.0 PG A:UTP602 3.4 29.1 1.0 O3A A:UTP602 3.5 27.6 1.0 OD2 A:ASP278 3.5 29.5 1.0 O A:HOH702 3.6 23.4 1.0 O3B A:UTP602 3.7 26.5 1.0 HA3 A:GLY266 3.8 24.0 1.0 C5' A:UTP602 3.9 25.0 1.0 H5'2 A:UTP602 3.9 30.0 1.0 O A:HOH758 4.0 35.5 1.0 OG A:SER267 4.1 23.9 1.0 O3G A:UTP602 4.2 25.6 1.0 O5' A:UTP602 4.2 28.4 1.0 O A:ASP278 4.2 25.7 1.0 N A:SER267 4.2 20.0 1.0 HG A:SER267 4.2 28.7 1.0 O A:HOH727 4.3 19.1 1.0 O1A A:UTP602 4.4 39.3 1.0 CB A:ASP280 4.5 24.9 1.0 H A:ASP278 4.5 28.7 1.0 H A:ASP280 4.5 25.6 1.0 CB A:ASP278 4.5 24.9 1.0 HB2 A:ASP280 4.6 29.9 1.0 HB3 A:SER267 4.6 30.3 1.0 C A:ASP278 4.6 26.0 1.0 O2B A:UTP602 4.6 27.2 1.0 CA A:GLY266 4.6 20.0 1.0 O2G A:UTP602 4.6 29.8 1.0 HA2 A:GLY266 4.7 24.0 1.0 HB3 A:SER277 4.8 30.2 1.0 CB A:SER267 4.8 25.3 1.0 N A:ASP278 4.9 23.9 1.0 N A:ASP280 4.9 21.3 1.0 CA A:ASP278 4.9 25.4 1.0 C A:GLY266 5.0 19.8 1.0 HB2 A:ASP278 5.0 29.9 1.0

L.Cheng, F.Li, Y.Jiang, H.Yu, C.Xie, Y.Shi, Q.Gong. Structural Insights Into A Unique Preference For 3' Terminal Guanine of Mirtron in Drosophila Tutase Tailor. Nucleic Acids Res. V. 47 495 2019.
ISSN: ESSN 1362-4962
PubMed: 30407553
DOI: 10.1093/NAR/GKY1116