Zinc in PDB 3oj4: Crystal Structure of the A20 ZNF4, Ubiquitin and UBCH5A Complex

All present enzymatic activity of Crystal Structure of the A20 ZNF4, Ubiquitin and UBCH5A Complex:
6.3.2.19;

The structure of Crystal Structure of the A20 ZNF4, Ubiquitin and UBCH5A Complex, PDB code: 3oj4 was solved by I.Bosanac, S.G.Hymowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 3.40
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	102.646, 102.646, 112.686, 90.00, 90.00, 120.00
R / Rfree (%)	28 / 31.9

The binding sites of Zinc atom in the Crystal Structure of the A20 ZNF4, Ubiquitin and UBCH5A Complex (pdb code 3oj4). 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 A20 ZNF4, Ubiquitin and UBCH5A Complex, PDB code: 3oj4:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the A20 ZNF4, Ubiquitin and UBCH5A 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 A20 ZNF4, Ubiquitin and UBCH5A Complex within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn900 b:73.0 occ:1.00 SG C:CYS607 2.3 38.4 1.0 SG C:CYS627 2.3 56.8 1.0 SG C:CYS612 2.3 47.0 1.0 SG C:CYS624 2.3 41.9 1.0 CB C:CYS607 3.2 36.3 1.0 CB C:CYS627 3.3 58.1 1.0 CB C:CYS612 3.3 58.9 1.0 CB C:CYS624 3.5 38.1 1.0 N C:CYS624 4.0 40.0 1.0 CB C:LYS609 4.2 73.4 1.0 CA C:CYS624 4.3 40.7 1.0 CA C:CYS627 4.5 69.5 1.0 N C:CYS627 4.6 66.2 1.0 CA C:CYS607 4.7 40.0 1.0 O C:CYS624 4.7 51.2 1.0 CA C:CYS612 4.8 70.7 1.0 C C:CYS624 4.8 47.8 1.0 CB C:TYR614 4.9 46.9 1.0 N C:LYS609 5.0 65.7 1.0 C C:CYS607 5.0 46.7 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the A20 ZNF4, Ubiquitin and UBCH5A 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 A20 ZNF4, Ubiquitin and UBCH5A Complex within 5.0Å range: probe atom residue distance (Å) B Occ F:Zn900 b:74.2 occ:1.00 SG F:CYS607 2.3 40.7 1.0 SG F:CYS627 2.3 56.5 1.0 SG F:CYS624 2.3 43.9 1.0 SG F:CYS612 2.3 49.9 1.0 CB F:CYS607 3.3 38.9 1.0 CB F:CYS627 3.3 57.8 1.0 CB F:CYS612 3.3 60.7 1.0 CB F:CYS624 3.4 40.3 1.0 N F:CYS624 4.0 42.0 1.0 CA F:CYS624 4.3 42.3 1.0 CB F:LYS609 4.3 73.0 1.0 CA F:CYS627 4.5 67.7 1.0 N F:CYS627 4.5 64.6 1.0 O F:CYS624 4.7 51.9 1.0 CA F:CYS607 4.7 42.7 1.0 CA F:CYS612 4.8 72.4 1.0 C F:CYS624 4.8 48.7 1.0 CB F:TYR614 4.8 48.3 1.0

I.Bosanac, I.E.Wertz, B.Pan, C.Yu, S.Kusam, C.Lam, L.Phu, Q.Phung, B.Maurer, D.Arnott, D.S.Kirkpatrick, V.M.Dixit, S.G.Hymowitz. Ubiquitin Binding to A20 ZNF4 Is Required For Modulation of Nf-κB Signaling Mol.Cell V. 40 548 2010.
ISSN: ISSN 1097-2765
PubMed: 21095585
DOI: 10.1016/J.MOLCEL.2010.10.009