Zinc in PDB 1uw0: Solution Structure of the Zinc-Finger Domain From Dna Ligase Iiia

All present enzymatic activity of Solution Structure of the Zinc-Finger Domain From Dna Ligase Iiia:
6.5.1.1;

The binding sites of Zinc atom in the Solution Structure of the Zinc-Finger Domain From Dna Ligase Iiia (pdb code 1uw0). 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 Solution Structure of the Zinc-Finger Domain From Dna Ligase Iiia, PDB code: 1uw0:

Zinc binding site 1 out of 1 in the Solution Structure of the Zinc-Finger Domain From Dna Ligase Iiia


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Solution Structure of the Zinc-Finger Domain From Dna Ligase Iiia within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1118 b:0.0 occ:1.00 ND1 A:HIS52 2.0 0.0 1.0 SG A:CYS18 2.3 0.0 1.0 SG A:CYS21 2.3 0.0 1.0 SG A:CYS55 2.3 0.0 1.0 HB2 A:HIS52 2.5 0.0 1.0 HB3 A:CYS18 2.7 0.0 1.0 CG A:HIS52 3.0 0.0 1.0 CB A:CYS18 3.0 0.0 1.0 CE1 A:HIS52 3.1 0.0 1.0 HB3 A:CYS21 3.2 0.0 1.0 CB A:HIS52 3.2 0.0 1.0 HB2 A:CYS55 3.3 0.0 1.0 CB A:CYS55 3.3 0.0 1.0 CB A:CYS21 3.3 0.0 1.0 HE1 A:HIS52 3.4 0.0 1.0 HB2 A:CYS18 3.5 0.0 1.0 H A:HIS52 3.6 0.0 1.0 HB3 A:CYS55 3.6 0.0 1.0 HB2 A:CYS21 3.7 0.0 1.0 HB3 A:GLU23 3.8 0.0 1.0 HB3 A:HIS52 3.9 0.0 1.0 O A:LYS19 4.1 0.0 1.0 N A:HIS52 4.1 0.0 1.0 CD2 A:HIS52 4.1 0.0 1.0 NE2 A:HIS52 4.2 0.0 1.0 CA A:HIS52 4.3 0.0 1.0 CA A:CYS18 4.3 0.0 1.0 H A:CYS55 4.5 0.0 1.0 C A:CYS18 4.5 0.0 1.0 HB2 A:GLU23 4.6 0.0 1.0 CB A:GLU23 4.7 0.0 1.0 CA A:CYS21 4.7 0.0 1.0 CA A:CYS55 4.7 0.0 1.0 HA A:TYR51 4.7 0.0 1.0 O A:CYS18 4.8 0.0 1.0 N A:LYS19 4.8 0.0 1.0 HA A:HIS52 4.8 0.0 1.0 H A:CYS18 4.9 0.0 1.0 H A:GLU23 4.9 0.0 1.0 N A:CYS21 4.9 0.0 1.0 H A:LYS19 4.9 0.0 1.0 C A:LYS19 5.0 0.0 1.0 N A:CYS55 5.0 0.0 1.0

A.W.Kulczyk, J.-C.Yang, D.Neuhaus. Solution Structure and Dna Binding of the Zinc-Finger Domain From Dna Ligase Iiialpha J.Mol.Biol. V. 341 723 2004.
ISSN: ISSN 0022-2836
PubMed: 15288782
DOI: 10.1016/J.JMB.2004.06.035