Manganese in PDB 1zct: Structure of Glycogenin Truncated at Residue 270 in A Complex with Udp

All present enzymatic activity of Structure of Glycogenin Truncated at Residue 270 in A Complex with Udp:
2.4.1.186;

The structure of Structure of Glycogenin Truncated at Residue 270 in A Complex with Udp, PDB code: 1zct was solved by T.D.Hurley, S.L.Stout, E.Miner, J.Zhou, P.J.Roach, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.60
Space group	P 64
Cell size a, b, c (Å), α, β, γ (°)	75.000, 75.000, 233.380, 90.00, 90.00, 120.00
R / Rfree (%)	23.9 / 25.3

The binding sites of Manganese atom in the Structure of Glycogenin Truncated at Residue 270 in A Complex with Udp (pdb code 1zct). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Structure of Glycogenin Truncated at Residue 270 in A Complex with Udp, PDB code: 1zct:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Structure of Glycogenin Truncated at Residue 270 in A Complex with Udp


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of Glycogenin Truncated at Residue 270 in A Complex with Udp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn400 b:49.5 occ:1.00 NE2 A:HIS211 2.1 42.3 1.0 O1B A:UDP411 2.2 53.3 1.0 OD2 A:ASP101 2.2 46.7 1.0 OD1 A:ASP103 2.3 46.9 1.0 O1A A:UDP411 2.4 52.6 1.0 OD2 A:ASP103 2.6 46.3 1.0 CG A:ASP103 2.8 50.5 1.0 CE1 A:HIS211 2.9 47.0 1.0 O3A A:UDP411 3.2 52.9 1.0 CG A:ASP101 3.2 50.0 1.0 CD2 A:HIS211 3.2 45.4 1.0 PB A:UDP411 3.2 58.2 1.0 PA A:UDP411 3.4 55.4 1.0 CB A:ASP101 3.5 47.6 1.0 O3B A:UDP411 3.7 55.6 1.0 O3' A:UDP411 4.0 54.1 1.0 O A:HOH431 4.0 47.1 1.0 ND1 A:HIS211 4.1 40.9 1.0 O5' A:UDP411 4.2 54.5 1.0 C5' A:UDP411 4.2 52.9 1.0 CG A:HIS211 4.3 43.8 1.0 OD1 A:ASP101 4.3 52.5 1.0 CB A:ASP103 4.4 45.4 1.0 O2B A:UDP411 4.5 58.3 1.0 NZ A:LYS217 4.6 50.7 1.0 C3' A:UDP411 4.6 49.9 1.0 O2A A:UDP411 4.7 55.6 1.0 O A:HOH430 4.7 60.9 1.0 C4' A:UDP411 4.8 51.3 1.0 CD1 A:LEU213 4.9 61.9 1.0 CA A:LEU213 4.9 60.8 1.0 CA A:ASP101 5.0 47.2 1.0

Manganese binding site 2 out of 2 in the Structure of Glycogenin Truncated at Residue 270 in A Complex with Udp


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of Glycogenin Truncated at Residue 270 in A Complex with Udp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn401 b:48.9 occ:1.00 NE2 B:HIS211 2.0 41.7 1.0 OD1 B:ASP103 2.3 50.3 1.0 O1B B:UDP412 2.3 49.8 1.0 OD2 B:ASP101 2.3 52.4 1.0 O1A B:UDP412 2.3 44.3 1.0 OD2 B:ASP103 2.7 46.9 1.0 CG B:ASP103 2.8 49.6 1.0 CE1 B:HIS211 2.9 44.3 1.0 CD2 B:HIS211 3.1 44.7 1.0 O3A B:UDP412 3.2 45.5 1.0 PB B:UDP412 3.3 53.1 1.0 CG B:ASP101 3.3 51.9 1.0 PA B:UDP412 3.3 53.2 1.0 CB B:ASP101 3.5 52.2 1.0 O3B B:UDP412 3.7 53.1 1.0 O3' B:UDP412 4.0 53.6 1.0 ND1 B:HIS211 4.1 43.5 1.0 CG B:HIS211 4.2 44.3 1.0 O5' B:UDP412 4.2 51.8 1.0 O B:HOH428 4.2 58.8 1.0 CB B:ASP103 4.3 42.5 1.0 C5' B:UDP412 4.3 51.9 1.0 NZ B:LYS217 4.4 56.5 1.0 OD1 B:ASP101 4.4 55.3 1.0 O2B B:UDP412 4.6 51.3 1.0 O2A B:UDP412 4.6 49.5 1.0 C3' B:UDP412 4.6 48.9 1.0 CA B:LEU213 4.8 59.3 1.0 C4' B:UDP412 4.9 52.5 1.0 CD1 B:LEU213 4.9 60.3 1.0 CA B:ASP101 5.0 51.8 1.0

T.D.Hurley, S.Stout, E.Miner, J.Zhou, P.J.Roach. Requirements For Catalysis in Mammalian Glycogenin. J.Biol.Chem. V. 280 23892 2005.
ISSN: ISSN 0021-9258
PubMed: 15849187
DOI: 10.1074/JBC.M502344200