Magnesium in PDB 4ldt: The Structure of H/CEOTUB1-Ubiquitin Aldehyde-UBCH5B~Ub

All present enzymatic activity of The Structure of H/CEOTUB1-Ubiquitin Aldehyde-UBCH5B~Ub:
3.4.19.12; 6.3.2.19;

The structure of The Structure of H/CEOTUB1-Ubiquitin Aldehyde-UBCH5B~Ub, PDB code: 4ldt was solved by R.Wiener, A.T.Dibello, P.M.Lombardi, C.M.Guzzo, X.Zhang, M.J.Matunis, C.Wolberger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.65 / 1.90
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	104.894, 131.612, 46.501, 90.00, 90.00, 90.00
R / Rfree (%)	19.2 / 22.3

The binding sites of Magnesium atom in the The Structure of H/CEOTUB1-Ubiquitin Aldehyde-UBCH5B~Ub (pdb code 4ldt). 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 The Structure of H/CEOTUB1-Ubiquitin Aldehyde-UBCH5B~Ub, PDB code: 4ldt:

Magnesium binding site 1 out of 1 in the The Structure of H/CEOTUB1-Ubiquitin Aldehyde-UBCH5B~Ub


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Structure of H/CEOTUB1-Ubiquitin Aldehyde-UBCH5B~Ub within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg101 b:42.1 occ:1.00 O B:HOH222 2.1 31.2 1.0 O B:HOH227 2.2 31.8 1.0 OD1 B:ASP32 2.2 31.8 1.0 O B:HOH220 2.2 43.1 1.0 O B:HOH221 2.3 40.4 1.0 CG B:ASP32 3.3 30.2 1.0 O B:HOH207 3.4 39.4 1.0 OD2 B:ASP32 3.6 33.9 1.0 O B:HOH228 4.0 40.5 1.0 O B:ALA28 4.2 18.3 1.0 OE1 B:GLN31 4.2 28.2 1.0 CB B:ASP32 4.6 28.0 1.0 N B:ASP32 4.9 24.5 1.0 CA B:ASP32 4.9 26.4 1.0 CD B:GLN31 4.9 26.1 1.0

R.Wiener, A.T.Dibello, P.M.Lombardi, C.M.Guzzo, X.Zhang, M.J.Matunis, C.Wolberger. E2 Ubiquitin-Conjugating Enzymes Regulate the Deubiquitinating Activity of OTUB1. Nat.Struct.Mol.Biol. V. 20 1033 2013.
ISSN: ISSN 1545-9993
PubMed: 23955022
DOI: 10.1038/NSMB.2655