Chlorine in PDB 7edd: Crystal Structure of A Serine Protease From Streptococcus Pyogenes

All present enzymatic activity of Crystal Structure of A Serine Protease From Streptococcus Pyogenes:
3.4.21.110;

The structure of Crystal Structure of A Serine Protease From Streptococcus Pyogenes, PDB code: 7edd was solved by C.Jobichen, J.Sivaraman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.37 / 2.90
Space group	P 62 2 2
Cell size a, b, c (Å), α, β, γ (°)	191.969, 191.969, 252.788, 90, 90, 120
R / Rfree (%)	19.5 / 25.5

The structure of Crystal Structure of A Serine Protease From Streptococcus Pyogenes also contains other interesting chemical elements:

Calcium	(Ca)	10 atoms
Magnesium	(Mg)	1 atom

The binding sites of Chlorine atom in the Crystal Structure of A Serine Protease From Streptococcus Pyogenes (pdb code 7edd). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of A Serine Protease From Streptococcus Pyogenes, PDB code: 7edd:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of A Serine Protease From Streptococcus Pyogenes


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of A Serine Protease From Streptococcus Pyogenes within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1720 b:10.7 occ:1.00 MG A:MG1718 1.5 11.5 1.0 O A:HOH1871 1.7 20.9 1.0 O A:HOH1869 2.0 42.2 1.0 O A:HOH1867 2.2 30.1 1.0 O A:HOH1872 2.5 25.7 1.0 O A:HOH1870 2.6 45.1 1.0 O A:HOH1868 2.7 40.1 1.0 CL A:CL1721 2.9 60.4 1.0 NH1 A:ARG524 4.3 77.6 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of A Serine Protease From Streptococcus Pyogenes


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of A Serine Protease From Streptococcus Pyogenes within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1721 b:60.4 occ:1.00 O A:HOH1871 2.2 20.9 1.0 MG A:MG1718 2.3 11.5 1.0 CL A:CL1720 2.9 10.7 1.0 O A:HOH1872 2.9 25.7 1.0 O A:HOH1870 3.0 45.1 1.0 O A:HOH1869 3.3 42.2 1.0 O A:SER387 4.4 39.7 1.0 O A:HOH1867 4.4 30.1 1.0 O A:ASP388 4.6 45.6 1.0 O A:HOH1868 4.7 40.1 1.0 C A:ASP388 4.8 44.4 1.0

C.Jobichen, T.Ying Chong, T.Hui Ling, J.Sivaraman. The Autocatalytic Cleavage Domain Is Not Required For the Activity of Scpc, A Virulence Protease From Streptococcus Pyogenes : A Structural Insight. Biochemistry 2021.
ISSN: ISSN 0006-2960
PubMed: 33929828
DOI: 10.1021/ACS.BIOCHEM.1C00185