Magnesium in PDB 4zgy: Structure of Human Ornithine Decarboxylase in Complex with A C- Terminal Fragment of Antizyme

Enzymatic activity of Structure of Human Ornithine Decarboxylase in Complex with A C- Terminal Fragment of Antizyme

All present enzymatic activity of Structure of Human Ornithine Decarboxylase in Complex with A C- Terminal Fragment of Antizyme:
4.1.1.17;

Protein crystallography data

The structure of Structure of Human Ornithine Decarboxylase in Complex with A C- Terminal Fragment of Antizyme, PDB code: 4zgy was solved by H.Y.Wu, N.L.Chan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.29 / 2.63
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.698, 73.368, 162.084, 90.00, 90.00, 90.00
R / Rfree (%) 20.3 / 25.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Human Ornithine Decarboxylase in Complex with A C- Terminal Fragment of Antizyme (pdb code 4zgy). 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 Structure of Human Ornithine Decarboxylase in Complex with A C- Terminal Fragment of Antizyme, PDB code: 4zgy:

Magnesium binding site 1 out of 1 in 4zgy

Go back to Magnesium Binding Sites List in 4zgy
Magnesium binding site 1 out of 1 in the Structure of Human Ornithine Decarboxylase in Complex with A C- Terminal Fragment of Antizyme


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Human Ornithine Decarboxylase in Complex with A C- Terminal Fragment of Antizyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:77.3
occ:1.00
 O1P A:PLP501 2.2 69.4 1.0
O A:PHE238 2.2 70.3 1.0
N A:PHE238 3.1 52.4 1.0
N A:TYR278 3.1 53.6 1.0
C A:PHE238 3.1 61.3 1.0
CG A:ARG277 3.4 62.8 1.0
CA A:PHE238 3.4 52.0 1.0
CB A:TYR278 3.4 56.9 1.0
N A:GLY276 3.4 49.1 1.0
N A:ARG277 3.5 40.1 1.0
CB A:PHE238 3.5 47.2 1.0
P A:PLP501 3.6 64.3 1.0
C A:GLY237 3.7 56.4 1.0
N A:GLY237 3.7 51.0 1.0
CA A:TYR278 3.8 56.6 1.0
CA A:PRO275 4.0 50.3 1.0
C A:GLY276 4.0 45.2 1.0
C A:ARG277 4.1 54.4 1.0
CA A:ARG277 4.1 53.1 1.0
O2P A:PLP501 4.2 69.4 1.0
CA A:GLY237 4.2 51.0 1.0
C A:PRO275 4.2 54.7 1.0
CD2 A:PHE238 4.2 55.3 1.0
CB A:PRO275 4.2 48.8 1.0
CA A:GLY276 4.3 45.8 1.0
O3P A:PLP501 4.3 57.7 1.0
CB A:ARG277 4.3 52.6 1.0
CG A:PHE238 4.4 52.5 1.0
N A:PRO239 4.4 61.0 1.0
CD A:ARG277 4.4 72.5 1.0
O A:GLY237 4.5 57.1 1.0
C A:GLY236 4.7 51.6 1.0
O4P A:PLP501 4.7 69.6 1.0
CG A:TYR278 4.8 54.6 1.0
O A:GLY276 4.8 49.7 1.0
CA A:GLY236 4.9 56.3 1.0
NE A:ARG277 4.9 73.6 1.0

Reference:

H.Y.Wu, S.F.Chen, J.Y.Hsieh, F.Chou, Y.H.Wang, W.T.Lin, P.Y.Lee, Y.J.Yu, L.Y.Lin, T.S.Lin, C.L.Lin, G.Y.Liu, S.R.Tzeng, H.C.Hung, N.L.Chan. Structural Basis of Antizyme-Mediated Regulation of Polyamine Homeostasis Proc.Natl.Acad.Sci.Usa V. 112 11229 2015.
ISSN: ESSN 1091-6490
PubMed: 26305948
DOI: 10.1073/PNAS.1508187112
Page generated: Mon Dec 14 19:57:06 2020

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