Chlorine in PDB 5to1: HTRA2 Exposed (L266R, F303A) Mutant

All present enzymatic activity of HTRA2 Exposed (L266R, F303A) Mutant:
3.4.21.108;

The structure of HTRA2 Exposed (L266R, F303A) Mutant, PDB code: 5to1 was solved by M.Merski, P.J.Barbosa Pereira, S.Macedo-Ribeiro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.80 / 1.69
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	84.180, 84.180, 126.772, 90.00, 90.00, 120.00
R / Rfree (%)	16.8 / 19.8

The binding sites of Chlorine atom in the HTRA2 Exposed (L266R, F303A) Mutant (pdb code 5to1). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the HTRA2 Exposed (L266R, F303A) Mutant, PDB code: 5to1:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the HTRA2 Exposed (L266R, F303A) Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of HTRA2 Exposed (L266R, F303A) Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl502 b:57.0 occ:1.00 O A:HOH629 3.3 35.3 1.0 N A:GLU217 3.3 33.4 1.0 CA A:TYR216 3.8 32.2 1.0 CD2 A:TYR216 3.9 46.9 1.0 C A:TYR216 4.1 36.3 1.0 CB A:TYR216 4.1 33.0 1.0 CB A:GLU217 4.2 40.3 1.0 O A:HOH752 4.2 69.5 1.0 CA A:GLU217 4.3 35.8 1.0 O A:GLU217 4.3 40.7 1.0 CG A:TYR216 4.5 37.8 1.0 O A:THR215 4.7 40.0 1.0 C A:GLU217 4.8 34.2 1.0 CE2 A:TYR216 4.9 49.8 1.0

Chlorine binding site 2 out of 2 in the HTRA2 Exposed (L266R, F303A) Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of HTRA2 Exposed (L266R, F303A) Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl503 b:40.9 occ:1.00 OH A:TYR428 2.9 40.4 1.0 O A:HOH747 3.2 42.3 1.0 N A:GLY363 3.2 32.7 1.0 N A:ILE362 3.3 34.8 1.0 CD1 A:TYR361 3.7 33.3 1.0 CE1 A:TYR428 3.8 36.5 1.0 CZ A:TYR428 3.8 38.2 1.0 CG1 A:ILE362 3.8 37.8 1.0 CA A:GLY363 4.0 38.2 1.0 CA A:TYR361 4.0 31.9 1.0 C A:ILE362 4.1 32.3 1.0 CA A:ILE362 4.1 32.6 1.0 C A:TYR361 4.1 33.4 1.0 N A:VAL364 4.2 35.4 1.0 CE1 A:TYR361 4.3 31.8 1.0 CG A:TYR361 4.3 36.1 1.0 CB A:PRO225 4.4 29.8 1.0 O A:HOH613 4.5 43.0 1.0 CB A:ILE362 4.6 35.9 1.0 CB A:TYR361 4.6 35.6 1.0 O A:VAL364 4.6 35.6 1.0 C A:GLY363 4.7 40.5 1.0 O A:ARG360 4.8 44.7 1.0 O A:HOH614 4.9 33.6 1.0

M.Merski, C.Moreira, R.M.Abreu, M.J.Ramos, P.A.Fernandes, L.M.Martins, P.J.B.Pereira, S.Macedo-Ribeiro. Molecular Motion Regulates the Activity of the Mitochondrial Serine Protease HTRA2. Cell Death Dis V. 8 E3119 2017.
ISSN: ISSN 2041-4889
PubMed: 29022916
DOI: 10.1038/CDDIS.2017.487