Zinc in PDB 8p66: Structural Basis of Aggregate Binding/Recognition By the Aaa+ Disaggregase Clpg

The binding sites of Zinc atom in the Structural Basis of Aggregate Binding/Recognition By the Aaa+ Disaggregase Clpg (pdb code 8p66). 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 Structural Basis of Aggregate Binding/Recognition By the Aaa+ Disaggregase Clpg, PDB code: 8p66:

Zinc binding site 1 out of 1 in the Structural Basis of Aggregate Binding/Recognition By the Aaa+ Disaggregase Clpg


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural Basis of Aggregate Binding/Recognition By the Aaa+ Disaggregase Clpg within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn101 b:0.0 occ:1.00 NE2 B:HIS34 2.0 0.0 1.0 SG B:CYS6 2.3 0.0 1.0 SG B:CYS9 2.3 0.0 1.0 SG B:CYS31 2.3 0.0 1.0 CE1 B:HIS34 2.4 0.0 1.0 HE1 B:HIS34 2.6 0.0 1.0 CD2 B:HIS34 3.0 0.0 1.0 HB2 B:CYS31 3.2 0.0 1.0 H B:CYS31 3.2 0.0 1.0 CB B:CYS6 3.3 0.0 1.0 HB2 B:GLN11 3.3 0.0 1.0 HB2 B:CYS6 3.3 0.0 1.0 HB3 B:CYS9 3.3 0.0 1.0 HB3 B:CYS6 3.4 0.0 1.0 CB B:CYS31 3.4 0.0 1.0 CB B:CYS9 3.4 0.0 1.0 ND1 B:HIS34 3.4 0.0 1.0 H B:CYS9 3.5 0.0 1.0 HD2 B:HIS34 3.5 0.0 1.0 CG B:HIS34 3.7 0.0 1.0 N B:CYS9 4.0 0.0 1.0 HB B:VAL8 4.0 0.0 1.0 O B:CYS9 4.0 0.0 1.0 N B:CYS31 4.0 0.0 1.0 H B:GLN11 4.0 0.0 1.0 CA B:CYS9 4.1 0.0 1.0 HB3 B:CYS31 4.2 0.0 1.0 HD1 B:HIS34 4.2 0.0 1.0 HB2 B:CYS9 4.3 0.0 1.0 CA B:CYS31 4.3 0.0 1.0 C B:CYS9 4.3 0.0 1.0 CB B:GLN11 4.4 0.0 1.0 HG2 B:GLN11 4.7 0.0 1.0 CA B:CYS6 4.7 0.0 1.0 HA B:LEU30 4.8 0.0 1.0 H B:VAL8 4.8 0.0 1.0 N B:GLN11 4.8 0.0 1.0 HG3 B:GLN11 4.9 0.0 1.0 O B:GLN11 4.9 0.0 1.0 HB3 B:GLN11 4.9 0.0 1.0 HB2 B:HIS34 4.9 0.0 1.0 HA B:CYS31 4.9 0.0 1.0 CG B:GLN11 4.9 0.0 1.0 CB B:HIS34 5.0 0.0 1.0

P.Katikaridis, B.Simon, T.Jenne, S.Moon, C.Lee, J.Hennig, A.Mogk. Structural Basis of Aggregate Binding By the Aaa+ Disaggregase Clpg. J.Biol.Chem. 05336 2023.
ISSN: ESSN 1083-351X
PubMed: 37827289
DOI: 10.1016/J.JBC.2023.105336