Zinc in PDB 4lad: Crystal Structure of the UBE2G2:Ring-G2BR Complex

All present enzymatic activity of Crystal Structure of the UBE2G2:Ring-G2BR Complex:
6.3.2.19;

The structure of Crystal Structure of the UBE2G2:Ring-G2BR Complex, PDB code: 4lad was solved by Y.-H.Liang, J.Li, R.Das, R.A.Byrd, X.Ji, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.12 / 2.30
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	58.246, 58.246, 158.431, 90.00, 90.00, 90.00
R / Rfree (%)	22.6 / 28.1

The binding sites of Zinc atom in the Crystal Structure of the UBE2G2:Ring-G2BR Complex (pdb code 4lad). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the UBE2G2:Ring-G2BR Complex, PDB code: 4lad:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the UBE2G2:Ring-G2BR Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the UBE2G2:Ring-G2BR Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn701 b:61.4 occ:1.00 ND1 B:HIS361 2.4 72.4 1.0 SG B:CYS364 2.4 64.8 1.0 CG B:HIS361 3.2 74.4 1.0 CE1 B:HIS361 3.3 74.9 1.0 CB B:CYS364 3.3 68.5 1.0 CB B:HIS361 3.4 71.2 1.0 N B:HIS361 4.2 70.5 1.0 CD2 B:HIS361 4.3 74.0 1.0 NE2 B:HIS361 4.4 78.3 1.0 CA B:HIS361 4.4 71.5 1.0 CA B:CYS364 4.8 71.6 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the UBE2G2:Ring-G2BR Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the UBE2G2:Ring-G2BR Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn702 b:82.8 occ:1.00 ND1 B:HIS358 2.3 87.1 1.0 SG B:CYS375 2.4 75.9 1.0 SG B:CYS378 2.5 90.8 1.0 SG B:CYS356 2.5 97.7 1.0 CB B:CYS356 3.2 99.1 1.0 CE1 B:HIS358 3.2 87.2 1.0 CG B:HIS358 3.3 83.9 1.0 CB B:CYS378 3.6 86.2 1.0 CB B:CYS375 3.6 80.9 1.0 CB B:HIS358 3.6 83.2 1.0 N B:CYS378 3.9 84.5 1.0 NE2 B:HIS358 4.4 86.8 1.0 CA B:CYS378 4.4 88.5 1.0 CA B:CYS356 4.4 97.5 1.0 N B:HIS358 4.4 93.6 1.0 CB B:THR377 4.4 78.4 1.0 CD2 B:HIS358 4.4 86.6 1.0 C B:CYS356 4.4 94.9 1.0 O B:CYS356 4.4 93.5 1.0 CA B:HIS358 4.6 91.4 1.0 C B:THR377 4.7 80.3 1.0 CA B:THR377 5.0 75.6 1.0 CA B:CYS375 5.0 81.3 1.0 CG2 B:THR377 5.0 80.0 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