Zinc in PDB 2lxh: uc(Nmr) Structure of the Ring Domain in Ubiquitin Ligase GP78

The binding sites of Zinc atom in the uc(Nmr) Structure of the Ring Domain in Ubiquitin Ligase GP78 (pdb code 2lxh). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the uc(Nmr) Structure of the Ring Domain in Ubiquitin Ligase GP78, PDB code: 2lxh:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the uc(Nmr) Structure of the Ring Domain in Ubiquitin Ligase GP78


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of uc(Nmr) Structure of the Ring Domain in Ubiquitin Ligase GP78 within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn900 b:0.0 occ:1.00 ND1 C:HIS361 2.1 0.0 1.0 SG C:CYS341 2.2 0.0 1.0 SG C:CYS364 2.3 0.0 1.0 SG C:CYS344 2.4 0.0 1.0 CE1 C:HIS361 2.7 0.0 1.0 CG C:HIS361 2.9 0.0 1.0 HB2 C:CYS341 2.9 0.0 1.0 HB2 C:HIS361 3.0 0.0 1.0 HE1 C:HIS361 3.0 0.0 1.0 CB C:CYS341 3.1 0.0 1.0 CB C:CYS364 3.5 0.0 1.0 CB C:HIS361 3.5 0.0 1.0 HB2 C:CYS364 3.5 0.0 1.0 HB3 C:CYS341 3.5 0.0 1.0 H C:HIS361 3.7 0.0 1.0 NE2 C:HIS361 3.7 0.0 1.0 H C:CYS344 3.7 0.0 1.0 CD2 C:HIS361 3.7 0.0 1.0 HB3 C:CYS364 3.8 0.0 1.0 CB C:CYS344 3.8 0.0 1.0 HB3 C:CYS344 3.8 0.0 1.0 HB3 C:HIS361 4.2 0.0 1.0 O C:TRP345 4.4 0.0 1.0 CA C:CYS341 4.4 0.0 1.0 HA C:CYS341 4.4 0.0 1.0 N C:HIS361 4.4 0.0 1.0 N C:CYS344 4.5 0.0 1.0 HE2 C:HIS361 4.5 0.0 1.0 H C:CYS364 4.6 0.0 1.0 HB2 C:CYS344 4.6 0.0 1.0 CA C:CYS344 4.6 0.0 1.0 CA C:HIS361 4.6 0.0 1.0 HD2 C:HIS361 4.7 0.0 1.0 HB C:ILE343 4.7 0.0 1.0 HG3 C:MET348 4.7 0.0 1.0 CA C:CYS364 4.8 0.0 1.0 H C:TRP345 4.8 0.0 1.0 C C:CYS344 4.9 0.0 1.0 H C:ILE343 4.9 0.0 1.0 N C:TRP345 5.0 0.0 1.0

Zinc binding site 2 out of 2 in the uc(Nmr) Structure of the Ring Domain in Ubiquitin Ligase GP78


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of uc(Nmr) Structure of the Ring Domain in Ubiquitin Ligase GP78 within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn901 b:0.0 occ:1.00 ND1 C:HIS358 2.1 0.0 1.0 SG C:CYS375 2.2 0.0 1.0 SG C:CYS356 2.2 0.0 1.0 HE1 C:HIS358 2.3 0.0 1.0 SG C:CYS378 2.4 0.0 1.0 CE1 C:HIS358 2.4 0.0 1.0 H C:CYS378 2.7 0.0 1.0 HB C:THR377 3.0 0.0 1.0 CG C:HIS358 3.3 0.0 1.0 HB2 C:CYS356 3.4 0.0 1.0 HB2 C:CYS378 3.4 0.0 1.0 CB C:CYS356 3.5 0.0 1.0 CB C:CYS378 3.5 0.0 1.0 NE2 C:HIS358 3.6 0.0 1.0 N C:CYS378 3.6 0.0 1.0 HB2 C:HIS358 3.8 0.0 1.0 H C:THR377 3.8 0.0 1.0 CB C:CYS375 3.9 0.0 1.0 HB3 C:CYS356 4.0 0.0 1.0 CD2 C:HIS358 4.0 0.0 1.0 CB C:THR377 4.1 0.0 1.0 HB2 C:CYS375 4.1 0.0 1.0 CA C:CYS378 4.2 0.0 1.0 CB C:HIS358 4.2 0.0 1.0 HE2 C:HIS358 4.3 0.0 1.0 HG22 C:THR377 4.3 0.0 1.0 HB3 C:CYS375 4.3 0.0 1.0 HB3 C:CYS378 4.4 0.0 1.0 HD2 C:PRO376 4.5 0.0 1.0 N C:THR377 4.6 0.0 1.0 C C:THR377 4.6 0.0 1.0 CA C:THR377 4.7 0.0 1.0 H C:GLY357 4.7 0.0 1.0 CG2 C:THR377 4.7 0.0 1.0 C C:CYS356 4.7 0.0 1.0 CA C:CYS356 4.7 0.0 1.0 N C:GLY357 4.7 0.0 1.0 HA C:CYS378 4.8 0.0 1.0 HA C:CYS375 4.8 0.0 1.0 C C:GLY357 4.9 0.0 1.0 CA C:CYS375 4.9 0.0 1.0 O C:GLY357 4.9 0.0 1.0 HB3 C:HIS358 4.9 0.0 1.0 H C:ARG379 4.9 0.0 1.0 HZ C:PHE360 4.9 0.0 1.0 HG23 C:THR377 4.9 0.0 1.0 OG1 C:THR377 5.0 0.0 1.0

R.Das, Y.H.Liang, J.Mariano, J.Li, T.Huang, A.King, S.G.Tarasov, A.M.Weissman, X.Ji, R.A.Byrd. Allosteric Regulation of E2:E3 Interactions Promote A Processive Ubiquitination Machine. Embo J. V. 32 2504 2013.
ISSN: ISSN 0261-4189
PubMed: 23942235
DOI: 10.1038/EMBOJ.2013.174