Zinc in PDB 2k3r: Pfu RPP21 Structure and Assignments

All present enzymatic activity of Pfu RPP21 Structure and Assignments:
3.1.26.5;

The binding sites of Zinc atom in the Pfu RPP21 Structure and Assignments (pdb code 2k3r). 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 Pfu RPP21 Structure and Assignments, PDB code: 2k3r:

Zinc binding site 1 out of 1 in the Pfu RPP21 Structure and Assignments


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Pfu RPP21 Structure and Assignments within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn124 b:0.0 occ:1.00 SG A:CYS92 2.3 0.0 1.0 SG A:CYS95 2.3 0.0 1.0 SG A:CYS63 2.3 0.0 1.0 SG A:CYS66 2.3 0.0 1.0 H A:CYS95 2.7 0.0 1.0 HB3 A:CYS92 2.7 0.0 1.0 HB3 A:CYS95 3.0 0.0 1.0 HB2 A:CYS66 3.1 0.0 1.0 CB A:CYS92 3.1 0.0 1.0 CB A:CYS95 3.1 0.0 1.0 CB A:CYS63 3.3 0.0 1.0 N A:CYS95 3.3 0.0 1.0 CB A:CYS66 3.3 0.0 1.0 HB2 A:CYS63 3.3 0.0 1.0 HB3 A:CYS63 3.4 0.0 1.0 O A:CYS92 3.6 0.0 1.0 HB2 A:GLU94 3.7 0.0 1.0 CA A:CYS95 3.8 0.0 1.0 H A:CYS66 3.8 0.0 1.0 HB2 A:CYS92 3.8 0.0 1.0 HG2 A:GLU94 3.9 0.0 1.0 HB3 A:CYS66 3.9 0.0 1.0 HB2 A:CYS95 4.1 0.0 1.0 C A:CYS92 4.1 0.0 1.0 CA A:CYS92 4.2 0.0 1.0 H A:GLU94 4.2 0.0 1.0 C A:GLU94 4.3 0.0 1.0 N A:CYS66 4.3 0.0 1.0 HD23 A:LEU70 4.4 0.0 1.0 HA A:CYS95 4.4 0.0 1.0 CA A:CYS66 4.4 0.0 1.0 H A:GLY96 4.4 0.0 1.0 CB A:GLU94 4.5 0.0 1.0 N A:GLU94 4.5 0.0 1.0 CG A:GLU94 4.7 0.0 1.0 H A:LYS65 4.7 0.0 1.0 CA A:CYS63 4.7 0.0 1.0 CA A:GLU94 4.7 0.0 1.0 H A:CYS92 4.7 0.0 1.0 HG2 A:LYS65 4.7 0.0 1.0 HB1 A:ALA68 4.8 0.0 1.0 HA A:CYS63 4.8 0.0 1.0 H A:HIS97 4.9 0.0 1.0 HD21 A:ASN75 4.9 0.0 1.0 HG3 A:LYS65 4.9 0.0 1.0 N A:CYS92 4.9 0.0 1.0 C A:CYS95 4.9 0.0 1.0 HA A:CYS66 4.9 0.0 1.0 HD22 A:LEU70 5.0 0.0 1.0 N A:LEU93 5.0 0.0 1.0 HA A:CYS92 5.0 0.0 1.0

C.D.Amero, W.P.Boomershine, Y.Xu, M.Foster. Solution Structure of Pyrococcus Furiosus RPP21, A Component of the Archaeal Rnase P Holoenzyme, and Interactions with Its RPP29 Protein Partner. Biochemistry V. 47 11704 2008.
ISSN: ISSN 0006-2960
PubMed: 18922021
DOI: 10.1021/BI8015982