Zinc in PDB 5a0s: Apo-Structure of Metalloprotease ZMP1 Variant E143A From Clostridium Difficile

The structure of Apo-Structure of Metalloprotease ZMP1 Variant E143A From Clostridium Difficile, PDB code: 5a0s was solved by M.Schacherl, C.Pichlo, I.Neundorf, U.Baumann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.86 / 2.56
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	43.500, 72.390, 118.530, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 26

The binding sites of Zinc atom in the Apo-Structure of Metalloprotease ZMP1 Variant E143A From Clostridium Difficile (pdb code 5a0s). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Apo-Structure of Metalloprotease ZMP1 Variant E143A From Clostridium Difficile, PDB code: 5a0s:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Apo-Structure of Metalloprotease ZMP1 Variant E143A From Clostridium Difficile


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Apo-Structure of Metalloprotease ZMP1 Variant E143A From Clostridium Difficile within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1221 b:28.2 occ:1.00 OE1 A:GLU185 2.1 20.8 1.0 NE2 A:HIS146 2.2 25.0 1.0 NE2 A:HIS142 2.4 18.8 1.0 O A:HOH2056 2.4 18.1 1.0 CD A:GLU185 2.8 22.8 1.0 OE2 A:GLU185 2.9 23.8 1.0 CD2 A:HIS142 3.1 14.4 1.0 CE1 A:HIS146 3.1 24.1 1.0 CD2 A:HIS146 3.2 24.8 1.0 CE1 A:HIS142 3.5 25.2 1.0 OH A:TYR178 4.0 26.7 1.0 ND1 A:HIS146 4.2 23.6 1.0 CG A:HIS146 4.3 22.6 1.0 CG A:GLU185 4.3 20.8 1.0 CG A:HIS142 4.3 15.8 1.0 ND1 A:HIS142 4.5 23.8 1.0 O A:HOH2035 4.7 12.4 1.0 CB A:ALA188 4.8 9.4 1.0 CE2 A:TYR178 4.9 25.9 1.0 CB A:GLU185 4.9 18.4 1.0 CA A:GLU185 4.9 18.9 1.0 CZ A:TYR178 4.9 22.8 1.0

Zinc binding site 2 out of 2 in the Apo-Structure of Metalloprotease ZMP1 Variant E143A From Clostridium Difficile


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Apo-Structure of Metalloprotease ZMP1 Variant E143A From Clostridium Difficile within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1221 b:32.4 occ:1.00 OE1 B:GLU185 2.1 18.5 1.0 NE2 B:HIS146 2.3 33.8 1.0 NE2 B:HIS142 2.3 14.4 1.0 CD B:GLU185 2.9 20.1 1.0 CD2 B:HIS142 3.0 14.5 1.0 OE2 B:GLU185 3.1 21.4 1.0 CD2 B:HIS146 3.2 32.0 1.0 CE1 B:HIS146 3.3 31.6 1.0 CE1 B:HIS142 3.4 17.4 1.0 O B:HOH2035 3.9 38.3 1.0 OH B:TYR178 4.0 17.2 1.0 CG B:HIS142 4.3 16.9 1.0 CG B:HIS146 4.3 28.0 1.0 ND1 B:HIS146 4.3 30.8 1.0 CG B:GLU185 4.4 13.3 1.0 ND1 B:HIS142 4.4 19.2 1.0 O B:HOH2019 4.5 37.7 1.0 CB B:GLU185 4.8 12.4 1.0 CB B:ALA188 5.0 12.4 1.0 CE2 B:TYR178 5.0 17.6 1.0

M.Schacherl, C.Pichlo, I.Neundorf, U.Baumann. Structural Basis of Proline-Proline Peptide Bond Specificity of the Metalloprotease ZMP1 Implicated in Motility of Clostridium Difficile. Structure V. 23 1632 2015.
ISSN: ISSN 0969-2126
PubMed: 26211609
DOI: 10.1016/J.STR.2015.06.018