Zinc in PDB 4rou: Auto-Inhibition Mechanism of Human Mitochondrial Rnase P Protein Complex

The structure of Auto-Inhibition Mechanism of Human Mitochondrial Rnase P Protein Complex, PDB code: 4rou was solved by F.Li, X.Liu, X.Yang, Y.Shen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.13 / 2.71
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	66.434, 78.287, 114.187, 90.00, 90.00, 90.00
R / Rfree (%)	23.8 / 27.8

The structure of Auto-Inhibition Mechanism of Human Mitochondrial Rnase P Protein Complex also contains other interesting chemical elements:

Chlorine

(Cl)

3 atoms

The binding sites of Zinc atom in the Auto-Inhibition Mechanism of Human Mitochondrial Rnase P Protein Complex (pdb code 4rou). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Auto-Inhibition Mechanism of Human Mitochondrial Rnase P Protein Complex, PDB code: 4rou:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Auto-Inhibition Mechanism of Human Mitochondrial Rnase P Protein Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Auto-Inhibition Mechanism of Human Mitochondrial Rnase P Protein Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn601 b:93.7 occ:1.00 SG B:CYS348 2.3 0.0 1.0 SG B:CYS351 2.3 0.0 1.0 SG B:CYS578 2.4 77.4 1.0 NE2 B:HIS557 2.5 55.4 1.0 CB B:CYS348 3.0 64.6 1.0 CD2 B:HIS557 3.2 50.9 1.0 N B:CYS351 3.3 83.6 1.0 CB B:CYS578 3.3 65.3 1.0 CB B:CYS351 3.5 85.0 1.0 CE1 B:HIS557 3.6 65.3 1.0 CA B:CYS351 4.0 79.3 1.0 C B:GLY350 4.2 83.4 1.0 CA B:GLY350 4.2 69.8 1.0 CA B:CYS578 4.2 52.6 1.0 N B:GLY350 4.3 68.4 1.0 CG B:HIS557 4.4 61.5 1.0 CA B:CYS348 4.4 62.5 1.0 ND1 B:HIS557 4.5 60.9 1.0 C B:CYS348 4.7 79.0 1.0 CG2 B:THR340 4.9 67.3 1.0 C B:CYS578 4.9 61.1 1.0 O B:CYS348 4.9 93.2 1.0

Zinc binding site 2 out of 2 in the Auto-Inhibition Mechanism of Human Mitochondrial Rnase P Protein Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Auto-Inhibition Mechanism of Human Mitochondrial Rnase P Protein Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:61.8 occ:1.00 NE2 A:HIS557 2.2 60.5 1.0 SG A:CYS578 2.4 62.3 1.0 SG A:CYS351 2.5 88.4 1.0 SG A:CYS348 2.5 68.8 1.0 CD2 A:HIS557 3.0 72.8 1.0 CE1 A:HIS557 3.2 59.3 1.0 CB A:CYS348 3.2 48.9 1.0 CB A:CYS351 3.3 50.6 1.0 CB A:CYS578 3.3 78.0 1.0 N A:CYS351 3.6 65.7 1.0 CA A:CYS351 4.0 56.0 1.0 CG A:HIS557 4.1 63.3 1.0 ND1 A:HIS557 4.2 57.0 1.0 CA A:CYS578 4.2 57.5 1.0 CA A:CYS348 4.6 56.0 1.0 C A:GLY350 4.7 76.2 1.0 CA A:GLY350 4.8 74.8 1.0 N A:GLY350 4.8 78.2 1.0 N A:GLY352 4.9 63.5 1.0 C A:CYS348 5.0 70.8 1.0 CG2 A:THR340 5.0 48.1 1.0 C A:CYS578 5.0 57.7 1.0

F.Li, X.Liu, X.Yang, Y.Shen. Auto-Inhibition Mechanism of Human Mitochondrial Rnase P Protein Complex To Be Published.