Zinc in PDB 4nql: The Crystal Structure of the Dub Domain of Amsh Orthologue, SST2 From S. Pombe, in Complex with Lysine 63-Linked Diubiquitin

The structure of The Crystal Structure of the Dub Domain of Amsh Orthologue, SST2 From S. Pombe, in Complex with Lysine 63-Linked Diubiquitin, PDB code: 4nql was solved by J.A.Ronau, R.K.Shrestha, C.Das, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.47 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	49.489, 56.740, 135.110, 90.00, 90.00, 90.00
R / Rfree (%)	21.3 / 26.3

The binding sites of Zinc atom in the The Crystal Structure of the Dub Domain of Amsh Orthologue, SST2 From S. Pombe, in Complex with Lysine 63-Linked Diubiquitin (pdb code 4nql). 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 The Crystal Structure of the Dub Domain of Amsh Orthologue, SST2 From S. Pombe, in Complex with Lysine 63-Linked Diubiquitin, PDB code: 4nql:

Zinc binding site 1 out of 1 in the The Crystal Structure of the Dub Domain of Amsh Orthologue, SST2 From S. Pombe, in Complex with Lysine 63-Linked Diubiquitin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Crystal Structure of the Dub Domain of Amsh Orthologue, SST2 From S. Pombe, in Complex with Lysine 63-Linked Diubiquitin within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:23.8 occ:1.00 NE2 A:HIS406 2.0 26.0 1.0 NE2 A:HIS356 2.2 22.1 1.0 NE2 A:HIS404 2.2 28.0 1.0 SG A:CYS397 2.3 30.8 1.0 CE1 A:HIS406 2.8 25.8 1.0 CD2 A:HIS404 3.1 28.3 1.0 CD2 A:HIS356 3.1 21.4 1.0 CD2 A:HIS406 3.2 27.2 1.0 CE1 A:HIS356 3.2 21.9 1.0 CE1 A:HIS404 3.3 28.2 1.0 CB A:CYS397 3.3 30.7 1.0 ND1 A:HIS406 3.9 26.4 1.0 CG A:HIS406 4.2 27.4 1.0 CG A:HIS404 4.3 29.0 1.0 ND1 A:HIS356 4.3 21.4 1.0 CG A:HIS356 4.3 20.7 1.0 ND1 A:HIS404 4.3 29.0 1.0 CD1 A:ILE394 4.4 22.2 1.0 CA A:CYS397 4.7 31.9 1.0 CB A:LYS399 4.8 40.6 1.0 CD A:LYS399 4.9 42.3 1.0

R.K.Shrestha, J.A.Ronau, C.W.Davies, R.G.Guenette, E.R.Strieter, L.N.Paul, C.Das. Insights Into the Mechanism of Deubiquitination By Jamm Deubiquitinases From Cocrystal Structures of the Enzyme with the Substrate and Product. Biochemistry V. 53 3199 2014.
ISSN: ISSN 0006-2960
PubMed: 24787148
DOI: 10.1021/BI5003162