Manganese in PDB 3u2u: Crystal Structure of Human Glycogenin-1 (GYG1) Complexed with Manganese, Udp and Maltotetraose

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

The structure of Crystal Structure of Human Glycogenin-1 (GYG1) Complexed with Manganese, Udp and Maltotetraose, PDB code: 3u2u was solved by A.Chaikuad, D.S.Froese, E.Krysztofinska, F.Von Delft, J.Weigelt, C.H.Arrowsmith, A.M.Edwards, C.Bountra, U.Oppermann, W.W.Yue, Structuralgenomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.20 / 1.45
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	46.765, 46.844, 69.848, 79.36, 88.45, 77.20
R / Rfree (%)	16.4 / 19.3

The binding sites of Manganese atom in the Crystal Structure of Human Glycogenin-1 (GYG1) Complexed with Manganese, Udp and Maltotetraose (pdb code 3u2u). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of Human Glycogenin-1 (GYG1) Complexed with Manganese, Udp and Maltotetraose, PDB code: 3u2u:
Jump to Manganese binding site number: 1; 2;

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


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Human Glycogenin-1 (GYG1) Complexed with Manganese, Udp and Maltotetraose within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn267 b:12.2 occ:1.00 OD2 A:ASP102 2.1 11.8 1.0 O1B A:UDP268 2.1 11.7 1.0 O1A A:UDP268 2.1 11.6 1.0 OD1 A:ASP104 2.1 11.8 1.0 OD2 A:ASP104 2.2 13.7 1.0 NE2 A:HIS212 2.2 10.8 1.0 CG A:ASP104 2.6 11.0 1.0 CG A:ASP102 3.2 11.2 1.0 CD2 A:HIS212 3.2 14.5 1.0 CE1 A:HIS212 3.2 12.0 1.0 PB A:UDP268 3.3 13.5 1.0 PA A:UDP268 3.4 13.1 1.0 CB A:ASP102 3.6 11.4 1.0 O3A A:UDP268 3.6 11.1 1.0 O3B A:UDP268 3.8 14.1 1.0 O3' A:UDP268 3.9 11.1 1.0 O2 A:GLC266 4.0 13.3 0.9 CB A:ASP104 4.1 12.2 1.0 C5' A:UDP268 4.2 12.1 1.0 O3 A:GLC266 4.2 14.2 0.9 OD1 A:ASP102 4.3 11.3 1.0 ND1 A:HIS212 4.3 12.2 1.0 CG A:HIS212 4.3 10.8 1.0 O5' A:UDP268 4.4 13.8 1.0 NZ A:LYS218 4.4 15.1 1.0 C3 A:GLC266 4.5 16.8 0.9 O2A A:UDP268 4.6 14.7 1.0 O2B A:UDP268 4.6 14.4 1.0 CA A:LEU214 4.6 20.1 1.0 C3' A:UDP268 4.7 10.5 1.0 C4' A:UDP268 4.9 9.5 1.0 N A:ASP104 4.9 10.3 1.0 C2 A:GLC266 4.9 14.1 0.9 CA A:ASP104 4.9 11.9 1.0 CB A:LEU214 5.0 20.0 1.0 N A:LEU214 5.0 15.7 1.0

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


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Human Glycogenin-1 (GYG1) Complexed with Manganese, Udp and Maltotetraose within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn267 b:11.4 occ:1.00 OD2 B:ASP102 2.0 11.1 1.0 O2A B:UDP268 2.1 11.2 1.0 O3B B:UDP268 2.1 10.0 1.0 OD1 B:ASP104 2.1 11.0 1.0 OD2 B:ASP104 2.1 13.2 1.0 NE2 B:HIS212 2.2 9.7 1.0 CG B:ASP104 2.6 9.9 1.0 CE1 B:HIS212 3.1 12.0 1.0 CD2 B:HIS212 3.1 14.6 1.0 CG B:ASP102 3.2 11.1 1.0 PB B:UDP268 3.3 11.9 1.0 PA B:UDP268 3.4 13.1 1.0 CB B:ASP102 3.6 10.2 1.0 O3A B:UDP268 3.6 11.8 1.0 O2B B:UDP268 3.9 12.0 1.0 O3' B:UDP268 3.9 11.8 1.0 O2 B:GLC266 4.0 13.9 0.9 CB B:ASP104 4.1 10.5 1.0 C5' B:UDP268 4.2 12.3 1.0 O3 B:GLC266 4.2 14.2 0.9 ND1 B:HIS212 4.3 10.3 1.0 OD1 B:ASP102 4.3 10.7 1.0 CG B:HIS212 4.3 11.6 1.0 O5' B:UDP268 4.3 12.7 1.0 NZ B:LYS218 4.4 15.7 1.0 C3 B:GLC266 4.5 15.9 0.9 O1A B:UDP268 4.5 14.2 1.0 O1B B:UDP268 4.5 15.2 1.0 CA B:LEU214 4.6 18.7 1.0 C3' B:UDP268 4.7 10.6 1.0 C4' B:UDP268 4.9 8.9 1.0 C2 B:GLC266 4.9 13.9 0.9 CB B:LEU214 4.9 20.5 1.0 N B:ASP104 4.9 10.2 1.0 CA B:ASP104 4.9 11.0 1.0 N B:LEU214 5.0 15.2 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