Zinc in PDB 4xgl: Structure of the Nuclease Subunit of Human Mitochondrial Rnase P (MRPP3) at 1.8A

All present enzymatic activity of Structure of the Nuclease Subunit of Human Mitochondrial Rnase P (MRPP3) at 1.8A:
3.1.26.5;

The structure of Structure of the Nuclease Subunit of Human Mitochondrial Rnase P (MRPP3) at 1.8A, PDB code: 4xgl was solved by L.Reinhard, S.Sridhara, B.M.Hallberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.63 / 1.80
Space group	P 43
Cell size a, b, c (Å), α, β, γ (°)	99.250, 99.250, 50.940, 90.00, 90.00, 90.00
R / Rfree (%)	18.9 / 22.8

The binding sites of Zinc atom in the Structure of the Nuclease Subunit of Human Mitochondrial Rnase P (MRPP3) at 1.8A (pdb code 4xgl). 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 the Nuclease Subunit of Human Mitochondrial Rnase P (MRPP3) at 1.8A, PDB code: 4xgl:

Zinc binding site 1 out of 1 in the Structure of the Nuclease Subunit of Human Mitochondrial Rnase P (MRPP3) at 1.8A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the Nuclease Subunit of Human Mitochondrial Rnase P (MRPP3) at 1.8A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:44.0 occ:1.00 NE2 A:HIS557 2.2 48.5 1.0 SG A:CYS578 2.4 46.5 1.0 SG A:CYS351 2.4 60.2 1.0 SG A:CYS348 2.6 53.5 1.0 CD2 A:HIS557 3.0 42.7 1.0 CB A:CYS348 3.1 47.4 1.0 CB A:CYS578 3.2 42.6 1.0 CE1 A:HIS557 3.3 49.4 1.0 CB A:CYS351 3.3 52.0 1.0 N A:CYS351 3.5 66.1 1.0 CA A:CYS351 4.0 59.8 1.0 CA A:CYS578 4.2 43.3 1.0 CG A:HIS557 4.2 42.1 1.0 ND1 A:HIS557 4.3 43.6 1.0 C A:GLY350 4.6 68.0 1.0 CA A:CYS348 4.6 51.5 1.0 O A:HOH835 4.6 63.5 1.0 CA A:GLY350 4.7 60.8 1.0 C A:CYS351 4.7 62.0 1.0 N A:GLY350 4.8 56.0 1.0 N A:GLY352 4.8 55.9 1.0 C A:CYS578 4.9 48.7 1.0

L.Reinhard, S.Sridhara, B.M.Hallberg. Structure of the Nuclease Subunit of Human Mitochondrial Rnase P. Nucleic Acids Res. 2015.
ISSN: ESSN 1362-4962
PubMed: 25953853
DOI: 10.1093/NAR/GKV481