Magnesium in PDB 9g09: Structure of Human RNF213 Bound to the Secreted Effector IPAH2.5 From Shigella Flexneri

All present enzymatic activity of Structure of Human RNF213 Bound to the Secreted Effector IPAH2.5 From Shigella Flexneri:
2.3.2.27;

The structure of Structure of Human RNF213 Bound to the Secreted Effector IPAH2.5 From Shigella Flexneri also contains other interesting chemical elements:

Zinc

(Zn)

3 atoms

The binding sites of Magnesium atom in the Structure of Human RNF213 Bound to the Secreted Effector IPAH2.5 From Shigella Flexneri (pdb code 9g09). 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 RNF213 Bound to the Secreted Effector IPAH2.5 From Shigella Flexneri, PDB code: 9g09:

Magnesium binding site 1 out of 1 in the Structure of Human RNF213 Bound to the Secreted Effector IPAH2.5 From Shigella Flexneri


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 RNF213 Bound to the Secreted Effector IPAH2.5 From Shigella Flexneri within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg5302 b:60.2 occ:1.00 O2B A:ATP5301 2.0 66.0 1.0 OE2 A:GLU2098 2.0 64.6 1.0 OG A:SER1999 2.0 62.7 1.0 CD A:GLU2098 3.0 64.6 1.0 O1G A:ATP5301 3.0 66.0 1.0 CB A:SER1999 3.4 62.7 1.0 OE1 A:GLU2098 3.4 64.6 1.0 PB A:ATP5301 3.5 66.0 1.0 O2G A:ATP5301 3.7 66.0 1.0 OD2 A:ASP2504 3.8 70.1 1.0 PG A:ATP5301 3.8 66.0 1.0 O3B A:ATP5301 4.2 66.0 1.0 O1A A:ATP5301 4.2 66.0 1.0 N A:SER1999 4.2 62.7 1.0 NH2 A:ARG2024 4.2 64.9 1.0 CG A:GLU2098 4.3 64.6 1.0 O3A A:ATP5301 4.3 66.0 1.0 CA A:SER1999 4.3 62.7 1.0 O1B A:ATP5301 4.4 66.0 1.0 NZ A:LYS2499 4.4 67.4 1.0 CG A:ASP2504 4.6 70.1 1.0 OD2 A:ASP2057 4.6 64.3 1.0 OD1 A:ASP2504 4.7 70.1 1.0 PA A:ATP5301 4.9 66.0 1.0

K.Naydenova, K.B.Boyle, C.Pathe, P.Pothukuchi, A.Crespillo-Casado, E.G.Otten, P.-M.Hammoudi, F.Randow. Shigella Flexneri Evades Lps Ubiquitylation Through IPAH1.4-Mediated Degradation of RNF213 To Be Published.