Zinc in PDB 1a6f: Rnase P Protein From Bacillus Subtilis

All present enzymatic activity of Rnase P Protein From Bacillus Subtilis:
3.1.26.5;

The structure of Rnase P Protein From Bacillus Subtilis, PDB code: 1a6f was solved by T.Stams, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.60
Space group	P 64
Cell size a, b, c (Å), α, β, γ (°)	82.400, 82.400, 33.500, 90.00, 90.00, 120.00
R / Rfree (%)	20.5 / 31.7

The binding sites of Zinc atom in the Rnase P Protein From Bacillus Subtilis (pdb code 1a6f). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Rnase P Protein From Bacillus Subtilis, PDB code: 1a6f:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Rnase P Protein From Bacillus Subtilis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Rnase P Protein From Bacillus Subtilis within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:65.3 occ:0.50 O A:HOH300 2.0 39.5 0.5 OE2 A:GLU40 2.0 46.6 1.0 O A:HOH301 2.2 32.7 0.5 OE1 A:GLN38 2.2 53.3 1.0 CD A:GLU40 3.2 47.7 1.0 CD A:GLN38 3.4 49.9 1.0 CG A:GLU40 4.1 46.0 1.0 OE1 A:GLU40 4.1 49.6 1.0 NE2 A:GLN38 4.1 50.9 1.0 CG A:GLN38 4.5 47.4 1.0 CB A:GLN38 4.5 46.2 1.0 CA A:GLN38 4.9 46.4 1.0

Zinc binding site 2 out of 2 in the Rnase P Protein From Bacillus Subtilis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Rnase P Protein From Bacillus Subtilis within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn202 b:49.6 occ:1.00 NE2 A:HIS22 1.8 35.1 1.0 O A:HOH302 2.2 19.8 1.0 CE1 A:HIS22 2.5 33.3 1.0 CD2 A:HIS22 3.0 32.5 1.0 ND1 A:HIS22 3.8 30.9 1.0 CG A:HIS22 4.0 31.8 1.0 CB A:LYS21 4.9 39.1 1.0

T.Stams, S.Niranjanakumari, C.A.Fierke, D.W.Christianson. Ribonuclease P Protein Structure: Evolutionary Origins in the Translational Apparatus. Science V. 280 752 1998.
ISSN: ISSN 0036-8075
PubMed: 9563955
DOI: 10.1126/SCIENCE.280.5364.752