Magnesium in PDB 6am0: Crystal Structure of K. Lactis EDC1-DCP1-DCP2-EDC3 Decapping Complex with Synthetic Cap Substrate Analog

The structure of Crystal Structure of K. Lactis EDC1-DCP1-DCP2-EDC3 Decapping Complex with Synthetic Cap Substrate Analog, PDB code: 6am0 was solved by J.S.Mugridge, J.D.Gross, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.96 / 2.84
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	174.260, 83.250, 104.300, 90.00, 93.62, 90.00
R / Rfree (%)	22.5 / 24.8

The binding sites of Magnesium atom in the Crystal Structure of K. Lactis EDC1-DCP1-DCP2-EDC3 Decapping Complex with Synthetic Cap Substrate Analog (pdb code 6am0). 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 Crystal Structure of K. Lactis EDC1-DCP1-DCP2-EDC3 Decapping Complex with Synthetic Cap Substrate Analog, PDB code: 6am0:

Magnesium binding site 1 out of 1 in the Crystal Structure of K. Lactis EDC1-DCP1-DCP2-EDC3 Decapping Complex with Synthetic Cap Substrate Analog


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of K. Lactis EDC1-DCP1-DCP2-EDC3 Decapping Complex with Synthetic Cap Substrate Analog within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:94.6 occ:1.00 OE1 A:GLU148 2.9 89.5 1.0 O20 A:6VQ302 3.4 0.9 1.0 NZ A:LYS134 3.5 0.2 1.0 CD A:GLU148 3.8 95.8 1.0 OE2 A:GLU197 3.9 0.1 1.0 CA A:GLY133 4.0 61.9 1.0 OE2 A:GLU148 4.1 0.8 1.0 NE2 A:GLN152 4.2 94.7 1.0 O A:ARG132 4.3 71.3 1.0 S24 A:6VQ302 4.3 0.3 1.0 N A:LYS134 4.5 64.7 1.0 CE A:LYS134 4.6 0.6 1.0 CD A:GLN152 4.8 82.6 1.0 C A:GLY133 4.9 69.0 1.0 P18 A:6VQ302 4.9 0.6 1.0 CG A:GLU148 5.0 91.3 1.0

J.S.Mugridge, R.W.Tibble, M.Ziemniak, J.Jemielity, J.D.Gross. Structure of the Activated EDC1-DCP1-DCP2-EDC3 Mrna Decapping Complex with Substrate Analog Poised For Catalysis. Nat Commun V. 9 1152 2018.
ISSN: ESSN 2041-1723
PubMed: 29559651
DOI: 10.1038/S41467-018-03536-X