Zinc in PDB 6r7w: Tannerella Forsythia Mature Mirolysin in Complex with A Cleaved Peptide.

The structure of Tannerella Forsythia Mature Mirolysin in Complex with A Cleaved Peptide., PDB code: 6r7w 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)	54.70 / 1.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	40.610, 66.490, 96.220, 90.00, 90.00, 90.00
R / Rfree (%)	14.4 / 15.8

The structure of Tannerella Forsythia Mature Mirolysin in Complex with A Cleaved Peptide. also contains other interesting chemical elements:

Calcium

(Ca)

2 atoms

The binding sites of Zinc atom in the Tannerella Forsythia Mature Mirolysin in Complex with A Cleaved Peptide. (pdb code 6r7w). 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 Mature Mirolysin in Complex with A Cleaved Peptide., PDB code: 6r7w:

Zinc binding site 1 out of 1 in the Tannerella Forsythia Mature Mirolysin in Complex with A Cleaved Peptide.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Tannerella Forsythia Mature Mirolysin in Complex with A Cleaved Peptide. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn403 b:8.9 occ:0.93 O5 A:CIT406 1.9 11.0 1.0 NE2 A:HIS228 2.0 8.6 1.0 NE2 A:HIS224 2.0 8.0 1.0 NE2 A:HIS234 2.0 9.4 1.0 C6 A:CIT406 2.6 11.8 1.0 O6 A:CIT406 2.6 11.6 1.0 CE1 A:HIS228 3.0 8.4 1.0 CD2 A:HIS224 3.0 8.7 1.0 CE1 A:HIS234 3.0 9.8 1.0 CD2 A:HIS234 3.0 8.9 1.0 CE1 A:HIS224 3.0 8.6 1.0 CD2 A:HIS228 3.1 9.3 1.0 O1 A:CIT406 3.9 14.3 1.0 CE1 A:TYR286 3.9 9.6 1.0 C3 A:CIT406 4.1 11.0 1.0 CG A:HIS234 4.1 8.6 1.0 ND1 A:HIS234 4.1 9.9 1.0 ND1 A:HIS228 4.1 9.7 1.0 CG A:HIS224 4.1 8.1 1.0 CG A:HIS228 4.2 9.3 1.0 ND1 A:HIS224 4.2 8.1 1.0 CA B:LYS1 4.3 9.4 1.0 N B:LYS1 4.3 9.6 1.0 OH A:TYR286 4.4 12.2 1.0 OE2 A:GLU225 4.4 13.7 1.0 O A:HOH520 4.6 20.1 1.0 O7 A:CIT406 4.6 13.6 1.0 C1 A:CIT406 4.6 13.2 1.0 CZ A:TYR286 4.6 11.9 1.0 CB B:LYS1 4.8 9.6 1.0 CE A:MET284 4.8 9.1 1.0 C2 A:CIT406 4.9 12.4 1.0 CD1 A:TYR286 4.9 10.3 1.0 C4 A:CIT406 4.9 11.8 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