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Manganese in PDB 3u2t: Crystal Structure of Human Glycogenin-1 (GYG1) Complexed with Manganese

Enzymatic activity of Crystal Structure of Human Glycogenin-1 (GYG1) Complexed with Manganese

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

Protein crystallography data

The structure of Crystal Structure of Human Glycogenin-1 (GYG1) Complexed with Manganese, PDB code: 3u2t 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) 36.99 / 2.05
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 58.350, 101.060, 47.830, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 25.1

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Human Glycogenin-1 (GYG1) Complexed with Manganese (pdb code 3u2t). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of Human Glycogenin-1 (GYG1) Complexed with Manganese, PDB code: 3u2t:

Manganese binding site 1 out of 1 in 3u2t

Go back to Manganese Binding Sites List in 3u2t
Manganese binding site 1 out of 1 in the Crystal Structure of Human Glycogenin-1 (GYG1) Complexed with Manganese


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn263

b:32.8
occ:1.00
OD2 A:ASP102 2.0 29.6 1.0
NE2 A:HIS212 2.1 25.0 1.0
OD1 A:ASP104 2.3 23.6 1.0
O A:HOH268 2.4 40.7 1.0
O A:HOH269 2.5 33.1 1.0
OD2 A:ASP104 2.5 26.2 1.0
CG A:ASP104 2.8 24.2 1.0
CG A:ASP102 3.0 24.4 1.0
CE1 A:HIS212 3.0 23.2 1.0
CD2 A:HIS212 3.2 19.8 1.0
CB A:ASP102 3.3 22.0 1.0
CD2 A:LEU214 4.0 36.4 1.0
OD1 A:ASP102 4.1 27.9 1.0
O A:HOH330 4.1 36.9 1.0
ND1 A:HIS212 4.2 22.8 1.0
CG A:HIS212 4.3 22.9 1.0
CB A:ASP104 4.3 25.0 1.0
O A:HOH342 4.3 47.2 1.0
O A:HOH326 4.3 36.6 1.0
O A:HOH345 4.4 42.9 1.0
NZ A:LYS218 4.6 27.3 1.0
CA A:ASP102 4.8 21.3 1.0
CA A:GLY135 4.8 21.0 1.0

Reference:

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
Page generated: Sat Oct 5 18:02:32 2024

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