Magnesium in PDB 3rmv: Crystal Structure of Human Glycogenin-1 (GYG1) T83M Mutant Complexed with Manganese and Udp

All present enzymatic activity of Crystal Structure of Human Glycogenin-1 (GYG1) T83M Mutant Complexed with Manganese and Udp:
2.4.1.186;

The structure of Crystal Structure of Human Glycogenin-1 (GYG1) T83M Mutant Complexed with Manganese and Udp, PDB code: 3rmv was solved by A.Chaikuad, D.S.Froese, W.W.Yue, E.Krysztofinska, F.Von Delft, J.Weigelt, C.H.Arrowsmith, A.M.Edwards, C.Bountra, U.Oppermann, Structural Genomicsconsortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.34 / 1.82
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	56.680, 100.720, 48.720, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 22.6

The structure of Crystal Structure of Human Glycogenin-1 (GYG1) T83M Mutant Complexed with Manganese and Udp also contains other interesting chemical elements:

Manganese

(Mn)

1 atom

The binding sites of Magnesium atom in the Crystal Structure of Human Glycogenin-1 (GYG1) T83M Mutant Complexed with Manganese and Udp (pdb code 3rmv). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Human Glycogenin-1 (GYG1) T83M Mutant Complexed with Manganese and Udp, PDB code: 3rmv:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Human Glycogenin-1 (GYG1) T83M Mutant Complexed with Manganese and Udp


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 Human Glycogenin-1 (GYG1) T83M Mutant Complexed with Manganese and Udp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg267 b:26.7 occ:0.60 MG A:MG267 0.0 26.7 0.6 O A:HOH469 1.6 38.7 1.0 MG A:MG267 1.8 12.4 0.4 OE2 A:GLU155 1.9 48.8 0.6 NE2 A:HIS151 2.1 40.8 1.0 O A:HOH472 2.3 45.9 1.0 CE1 A:HIS151 2.6 37.5 1.0 OE2 A:GLU155 2.8 42.6 0.4 CD A:GLU155 3.2 44.5 0.6 CD A:GLU155 3.2 46.4 0.4 O A:HOH473 3.3 51.7 1.0 CD2 A:HIS151 3.3 36.0 1.0 OE1 A:GLU155 3.5 45.4 0.4 ND1 A:HIS151 3.8 38.1 1.0 O A:HOH471 4.0 46.2 1.0 OE1 A:GLU155 4.0 43.1 0.6 O A:HOH466 4.1 45.4 1.0 CG A:HIS151 4.2 32.1 1.0 CG A:GLU155 4.2 40.0 0.6 CG A:GLU155 4.3 38.6 0.4 O A:HOH470 4.8 42.4 1.0 O A:HOH459 4.9 47.3 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Human Glycogenin-1 (GYG1) T83M Mutant Complexed with Manganese and Udp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Human Glycogenin-1 (GYG1) T83M Mutant Complexed with Manganese and Udp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg267 b:12.4 occ:0.40 MG A:MG267 0.0 12.4 0.4 OE2 A:GLU155 1.5 48.8 0.6 O A:HOH473 1.6 51.7 1.0 MG A:MG267 1.8 26.7 0.6 O A:HOH472 1.8 45.9 1.0 OE2 A:GLU155 1.9 42.6 0.4 NE2 A:HIS151 2.1 40.8 1.0 CD A:GLU155 2.3 44.5 0.6 OE1 A:GLU155 2.6 43.1 0.6 O A:HOH469 2.7 38.7 1.0 CD A:GLU155 2.9 46.4 0.4 CD2 A:HIS151 3.0 36.0 1.0 CE1 A:HIS151 3.1 37.5 1.0 O A:HOH470 3.7 42.4 1.0 CG A:GLU155 3.7 40.0 0.6 OE1 A:GLU155 3.7 45.4 0.4 CG A:GLU155 3.8 38.6 0.4 CG A:HIS151 4.1 32.1 1.0 ND1 A:HIS151 4.2 38.1 1.0 O A:HOH415 4.5 43.0 1.0 CB A:GLU155 4.6 34.2 0.6 CB A:GLU155 4.6 33.8 0.4 O A:HOH471 4.8 46.2 1.0 O A:HOH459 5.0 47.3 1.0

A.Chaikuad, D.S.Froese, G.Berridge, F.Von Delft, U.Oppermann, W.W.Yue. Conformational Plasticity of Glycogenin and Its Maltosaccharide Substrate During Glycogen Biogenesis. Proc.Natl.Acad.Sci.Usa V. 108 21028 2011.
ISSN: ISSN 0027-8424
PubMed: 22160680
DOI: 10.1073/PNAS.1113921108