Chlorine in PDB 4q7z: Neutrophil Serine Protease 4 (PRSS57) with Phe-Phe-Arg- Chloromethylketone (Ffr-Cmk)

The structure of Neutrophil Serine Protease 4 (PRSS57) with Phe-Phe-Arg- Chloromethylketone (Ffr-Cmk), PDB code: 4q7z was solved by C.Eigenbrot, S.J.Lin, K.C.Dong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.91 / 1.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.986, 64.466, 68.383, 90.00, 90.00, 90.00
R / Rfree (%)	19.2 / 21.5

The binding sites of Chlorine atom in the Neutrophil Serine Protease 4 (PRSS57) with Phe-Phe-Arg- Chloromethylketone (Ffr-Cmk) (pdb code 4q7z). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Neutrophil Serine Protease 4 (PRSS57) with Phe-Phe-Arg- Chloromethylketone (Ffr-Cmk), PDB code: 4q7z:

Chlorine binding site 1 out of 1 in the Neutrophil Serine Protease 4 (PRSS57) with Phe-Phe-Arg- Chloromethylketone (Ffr-Cmk)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Neutrophil Serine Protease 4 (PRSS57) with Phe-Phe-Arg- Chloromethylketone (Ffr-Cmk) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl306 b:24.1 occ:1.00 O A:HOH500 2.7 27.4 1.0 O A:HOH585 3.0 24.9 1.0 O A:HOH530 3.1 21.7 1.0 N A:ARG50 3.3 14.8 1.0 N A:ALA49 3.5 15.0 1.0 CB A:ARG48 3.7 13.2 0.5 CB A:ARG48 3.7 14.6 0.5 CB A:ARG50 3.7 23.6 1.0 CA A:ALA49 4.0 14.9 1.0 CD1 A:TRP51 4.0 13.9 1.0 CB A:ALA49 4.1 15.3 1.0 C A:ALA49 4.1 15.7 1.0 CA A:ARG50 4.1 17.1 1.0 C A:ARG48 4.1 12.9 1.0 CA A:ARG48 4.5 13.2 0.5 CA A:ARG48 4.5 12.7 0.5 NE1 A:TRP51 4.5 15.4 1.0 CG A:ARG48 4.7 16.5 0.5 CG A:ARG48 4.7 14.0 0.5 O A:HOH536 4.7 26.9 1.0 NE A:ARG48 4.8 14.9 0.5 C A:ARG50 4.9 15.1 1.0 O A:ARG48 4.9 13.1 1.0 OG A:SER111 5.0 23.1 1.0

S.J.Lin, K.C.Dong, C.Eigenbrot, M.Van Lookeren Campagne, D.Kirchhofer. Structures of Neutrophil Serine Protease 4 Reveal An Unusual Mechanism of Substrate Recognition By A Trypsin-Fold Protease. Structure V. 22 1333 2014.
ISSN: ISSN 0969-2126
PubMed: 25156428
DOI: 10.1016/J.STR.2014.07.008