Zinc in PDB 2wwz: TAB2 Nzf Domain in Complex with LYS63-Linked Di-Ubiquitin, P212121

The structure of TAB2 Nzf Domain in Complex with LYS63-Linked Di-Ubiquitin, P212121, PDB code: 2wwz was solved by Y.Kulathu, M.Akutsu, A.Bremm, K.Hofmann, D.Komander, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.19 / 1.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	30.980, 69.610, 71.520, 90.00, 90.00, 90.00
R / Rfree (%)	17.8 / 20.2

The binding sites of Zinc atom in the TAB2 Nzf Domain in Complex with LYS63-Linked Di-Ubiquitin, P212121 (pdb code 2wwz). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the TAB2 Nzf Domain in Complex with LYS63-Linked Di-Ubiquitin, P212121, PDB code: 2wwz:

Zinc binding site 1 out of 1 in the TAB2 Nzf Domain in Complex with LYS63-Linked Di-Ubiquitin, P212121


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of TAB2 Nzf Domain in Complex with LYS63-Linked Di-Ubiquitin, P212121 within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1694 b:10.1 occ:1.00 SG C:CYS673 2.3 9.5 1.0 SG C:CYS687 2.3 11.5 1.0 SG C:CYS670 2.4 9.6 1.0 SG C:CYS684 2.4 9.0 1.0 CB C:CYS684 3.1 9.4 1.0 CB C:CYS670 3.1 10.7 1.0 CB C:CYS673 3.3 10.3 1.0 CB C:CYS687 3.4 12.2 1.0 N C:CYS673 3.8 11.1 1.0 N C:CYS687 3.8 12.1 1.0 CA C:CYS673 4.1 10.2 1.0 CA C:CYS687 4.1 11.0 1.0 CB C:ALA672 4.5 12.5 1.0 CA C:CYS684 4.5 10.6 1.0 CB C:GLN686 4.6 11.2 1.0 CA C:CYS670 4.6 10.1 1.0 C C:ALA672 4.7 12.5 1.0 CB C:PHE675 4.7 8.1 1.0 C C:CYS673 4.7 9.2 1.0 N C:THR674 4.8 10.8 1.0 C C:CYS687 4.8 11.3 1.0 C C:GLN686 4.8 11.3 1.0 N C:PHE675 4.9 8.4 1.0 N C:GLU688 4.9 11.6 1.0 CA C:ALA672 5.0 12.0 1.0 N C:ALA672 5.0 11.6 1.0

Y.Kulathu, M.Akutsu, A.Bremm, K.Hofmann, D.Komander. Two-Sided Ubiquitin Binding Explains Specificity of the TAB2 Nzf Domain Nat.Struct.Mol.Biol. V. 16 1328 2009.
ISSN: ISSN 1545-9993
PubMed: 19935683
DOI: 10.1038/NSMB.1731