Zinc in PDB 6r7v: Tannerella Forsythia Promirolysin Mutant E225A

The structure of Tannerella Forsythia Promirolysin Mutant E225A, PDB code: 6r7v was solved by A.Rodriguez-Banqueri, T.Guevara, M.Ksiazek, J.Potempa, F.X.Gomis-Ruth, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.34 / 1.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	47.330, 67.250, 79.640, 90.00, 90.00, 90.00
R / Rfree (%)	16.1 / 18.8

The structure of Tannerella Forsythia Promirolysin Mutant E225A also contains other interesting chemical elements:

Calcium

(Ca)

2 atoms

The binding sites of Zinc atom in the Tannerella Forsythia Promirolysin Mutant E225A (pdb code 6r7v). 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 Tannerella Forsythia Promirolysin Mutant E225A, PDB code: 6r7v:

Zinc binding site 1 out of 1 in the Tannerella Forsythia Promirolysin Mutant E225A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Tannerella Forsythia Promirolysin Mutant E225A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn403 b:16.4 occ:0.74 NE2 A:HIS224 2.0 13.4 1.0 NE2 A:HIS234 2.0 15.0 1.0 NE2 A:HIS228 2.0 14.1 1.0 SG A:CYS23 2.2 17.9 1.0 CD2 A:HIS224 2.9 13.6 1.0 CD2 A:HIS234 3.0 14.9 1.0 CE1 A:HIS228 3.0 13.9 1.0 CD2 A:HIS228 3.1 13.9 1.0 CE1 A:HIS234 3.1 15.2 1.0 CE1 A:HIS224 3.1 14.2 1.0 CB A:CYS23 3.2 16.3 1.0 O A:HOH746 4.0 23.7 1.0 CG A:HIS224 4.1 14.0 1.0 CG A:HIS234 4.1 15.1 1.0 ND1 A:HIS234 4.1 16.0 1.0 ND1 A:HIS228 4.2 13.9 1.0 CG A:HIS228 4.2 13.4 1.0 ND1 A:HIS224 4.2 14.3 1.0 CE1 A:TYR286 4.2 19.8 1.0 CB A:SER25 4.5 16.8 1.0 O A:SER25 4.5 19.4 1.0 OH A:TYR286 4.6 22.7 1.0 CA A:CYS23 4.6 17.3 1.0 C A:SER25 4.8 20.3 1.0 N A:SER25 4.8 17.7 1.0 CE A:MET284 4.8 13.6 1.0 CA A:SER25 4.9 16.3 1.0 CZ A:TYR286 4.9 22.6 1.0

T.Guevara, A.Rodriguez-Banqueri, M.Ksiazek, J.Potempa, F.X.Gomis-Ruth. Structure-Based Mechanism of Cysteine-Switch Latency and of Catalysis By Pappalysin-Family Metallopeptidases Iucrj 2019.
ISSN: ESSN 2052-2525