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

Enzymatic activity of 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;

Protein crystallography data

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

Magnesium Binding Sites:

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 4ldt

Go back to Magnesium Binding Sites List in 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

Reference:

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
Page generated: Mon Dec 14 19:07:02 2020

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