Zinc in PDB 7onu: Structure of Human Mitochondrial Rnase P in Complex with Mitochondrial Pre-Trna-Tyr

All present enzymatic activity of Structure of Human Mitochondrial Rnase P in Complex with Mitochondrial Pre-Trna-Tyr:
1.1.1.159; 1.1.1.178; 1.1.1.239; 1.1.1.35; 1.1.1.53; 1.1.1.62; 2.1.1.218; 2.1.1.221; 3.1.26.5;

The structure of Structure of Human Mitochondrial Rnase P in Complex with Mitochondrial Pre-Trna-Tyr also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Zinc atom in the Structure of Human Mitochondrial Rnase P in Complex with Mitochondrial Pre-Trna-Tyr (pdb code 7onu). 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 Structure of Human Mitochondrial Rnase P in Complex with Mitochondrial Pre-Trna-Tyr, PDB code: 7onu:

Zinc binding site 1 out of 1 in the Structure of Human Mitochondrial Rnase P in Complex with Mitochondrial Pre-Trna-Tyr


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Human Mitochondrial Rnase P in Complex with Mitochondrial Pre-Trna-Tyr within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn601 b:145.0 occ:1.00 NE2 E:HIS557 2.1 101.5 1.0 SG E:CYS351 2.3 115.7 1.0 SG E:CYS348 2.3 112.3 1.0 SG E:CYS578 2.3 107.6 1.0 CE1 E:HIS557 2.6 101.5 1.0 CD2 E:HIS557 3.3 101.5 1.0 CE1 E:HIS580 3.5 113.9 1.0 NE2 E:HIS580 3.6 113.9 1.0 CB E:CYS578 3.7 107.6 1.0 CB E:CYS351 3.8 115.7 1.0 ND1 E:HIS557 3.9 101.5 1.0 CB E:CYS348 4.1 112.3 1.0 N E:CYS351 4.1 115.7 1.0 CG E:HIS557 4.2 101.5 1.0 CA E:CYS351 4.5 115.7 1.0 CB E:LYS353 4.6 110.1 1.0 ND1 E:HIS580 4.8 113.9 1.0 OG E:SER555 4.8 105.6 1.0 N E:LYS353 4.9 110.1 1.0 CD2 E:HIS580 4.9 113.9 1.0 C E:GLY350 4.9 113.6 1.0 CA E:CYS578 4.9 107.6 1.0 CD E:LYS353 4.9 110.1 1.0 N E:GLY352 5.0 113.4 1.0

A.Bhatta, C.Dienemann, P.Cramer, H.S.Hillen. Structural Basis of Rna Processing By Human Mitochondrial Rnase P Nat.Struct.Mol.Biol. 2021.
ISSN: ESSN 1545-9985
DOI: 10.1038/S41594-021-00637-Y