Chlorine in PDB 6can: Prolyl Oligopeptidase Mutant S477C From Pyrococcus Furiosus

The structure of Prolyl Oligopeptidase Mutant S477C From Pyrococcus Furiosus, PDB code: 6can was solved by K.Ellis-Guardiola, J.C.Lewis, N.Sukumar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	56.292, 178.764, 59.293, 90.00, 104.35, 90.00
R / Rfree (%)	19.6 / 25.1

The binding sites of Chlorine atom in the Prolyl Oligopeptidase Mutant S477C From Pyrococcus Furiosus (pdb code 6can). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 6 binding sites of Chlorine where determined in the Prolyl Oligopeptidase Mutant S477C From Pyrococcus Furiosus, PDB code: 6can:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6;

Chlorine binding site 1 out of 6 in the Prolyl Oligopeptidase Mutant S477C From Pyrococcus Furiosus


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Prolyl Oligopeptidase Mutant S477C From Pyrococcus Furiosus within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl701 b:39.5 occ:1.00 OH A:TYR555 2.8 26.3 1.0 NH1 A:ARG600 3.2 38.9 1.0 NH1 A:ARG476 3.4 35.0 1.0 NH2 A:ARG600 3.5 34.5 1.0 CD A:ARG476 3.6 36.4 1.0 CZ A:TYR555 3.7 32.9 1.0 CE2 A:TYR555 3.7 30.5 1.0 CZ A:ARG600 3.8 38.8 1.0 CZ2 A:TRP474 4.0 33.2 1.0 CD1 A:LEU607 4.2 29.3 1.0 CG A:ARG476 4.3 34.2 1.0 CZ A:ARG476 4.4 42.6 1.0 CD2 A:LEU604 4.4 29.9 1.0 NE A:ARG476 4.5 40.2 1.0 NE1 A:TRP474 4.5 27.5 1.0 CB A:ARG476 4.5 27.6 1.0 O A:HOH1055 4.6 51.9 1.0 CE2 A:TRP474 4.6 33.3 1.0 O A:HOH1162 4.6 45.5 1.0 CE1 A:TYR555 5.0 27.7 1.0

Chlorine binding site 2 out of 6 in the Prolyl Oligopeptidase Mutant S477C From Pyrococcus Furiosus


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Prolyl Oligopeptidase Mutant S477C From Pyrococcus Furiosus within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl702 b:58.1 occ:1.00 O A:HOH811 2.5 46.6 1.0 O A:HOH1186 3.3 42.8 1.0 OH A:TYR401 3.3 34.2 1.0 CE2 A:PHE404 3.6 35.9 1.0 NE1 A:TRP518 3.7 39.4 1.0 CZ A:PHE404 3.7 35.9 1.0 CD2 A:PHE404 3.8 31.5 1.0 SG A:CYS477 4.0 57.4 1.0 CE1 A:PHE404 4.1 35.7 1.0 CG A:PHE404 4.1 32.1 1.0 CD1 A:TRP518 4.3 32.7 1.0 CD1 A:PHE404 4.3 27.8 1.0 CE2 A:TRP518 4.3 37.3 1.0 CZ A:TYR401 4.6 31.5 1.0 CZ2 A:TRP518 4.7 35.7 1.0 CB A:ASN478 4.7 32.1 1.0

Chlorine binding site 3 out of 6 in the Prolyl Oligopeptidase Mutant S477C From Pyrococcus Furiosus


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Prolyl Oligopeptidase Mutant S477C From Pyrococcus Furiosus within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl703 b:62.4 occ:1.00 OE1 A:GLU603 2.8 37.7 1.0 O A:HOH915 3.1 38.7 1.0 OH A:TYR501 3.2 39.3 1.0 NH1 A:ARG476 3.3 35.0 1.0 NH2 A:ARG476 3.6 40.9 1.0 O A:HOH1109 3.7 54.6 1.0 O A:MET593 3.7 84.0 1.0 CZ A:TYR501 3.7 38.4 1.0 CD A:GLU603 3.8 37.5 1.0 CD A:ARG600 3.9 40.4 1.0 CZ A:ARG476 3.9 42.6 1.0 NH1 A:ARG600 3.9 38.9 1.0 CE1 A:TYR501 4.0 38.4 1.0 OE2 A:GLU603 4.0 36.8 1.0 NE A:ARG600 4.2 38.2 1.0 CZ A:ARG600 4.2 38.8 1.0 C A:MET593 4.6 85.1 1.0 CE2 A:TYR501 4.6 31.6 1.0

Chlorine binding site 4 out of 6 in the Prolyl Oligopeptidase Mutant S477C From Pyrococcus Furiosus


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Prolyl Oligopeptidase Mutant S477C From Pyrococcus Furiosus within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl701 b:39.0 occ:1.00 OH B:TYR555 3.1 27.1 1.0 NH1 B:ARG476 3.2 47.9 1.0 O B:HOH1134 3.3 42.8 1.0 NH2 B:ARG600 3.4 40.4 1.0 NH1 B:ARG600 3.4 43.7 1.0 CD B:ARG476 3.6 37.5 1.0 CZ B:ARG600 3.8 41.7 1.0 CE2 B:TYR555 3.9 29.0 1.0 CZ2 B:TRP474 3.9 27.2 1.0 CZ B:TYR555 4.0 26.9 1.0 CZ B:ARG476 4.2 49.0 1.0 CD2 B:LEU604 4.3 30.4 1.0 NE B:ARG476 4.4 40.4 1.0 CD1 B:LEU607 4.4 28.1 1.0 NE1 B:TRP474 4.6 27.8 1.0 CE2 B:TRP474 4.6 29.6 1.0 CB B:ARG476 4.7 34.7 1.0 CG B:ARG476 4.7 43.6 1.0 CH2 B:TRP474 4.9 28.8 1.0

Chlorine binding site 5 out of 6 in the Prolyl Oligopeptidase Mutant S477C From Pyrococcus Furiosus


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Prolyl Oligopeptidase Mutant S477C From Pyrococcus Furiosus within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl702 b:53.1 occ:1.00 O B:HOH1076 2.8 48.1 1.0 SG B:CYS477 3.1 64.8 1.0 O B:HOH842 3.3 54.2 1.0 OH B:TYR401 3.7 39.8 1.0 NE1 B:TRP518 4.0 40.5 1.0 CE2 B:PHE404 4.0 35.2 1.0 CE2 B:TRP518 4.1 42.3 1.0 CZ2 B:TRP518 4.2 38.5 1.0 CD2 B:PHE404 4.2 34.7 1.0 O B:HOH1004 4.3 54.7 1.0 CZ B:PHE404 4.4 33.0 1.0 CB B:CYS477 4.5 38.9 1.0 N B:ASN478 4.6 32.1 1.0 O B:HOH1144 4.7 50.2 1.0 CD1 B:TRP518 4.7 36.5 1.0 CB B:ASN478 4.7 33.1 1.0 CG B:PHE404 4.8 33.9 1.0 O B:HOH1165 4.8 47.2 1.0 NH2 B:ARG562 4.9 71.1 1.0 CD2 B:TRP518 4.9 34.8 1.0 CE1 B:PHE404 4.9 33.0 1.0 CZ B:TYR401 5.0 31.8 1.0

Chlorine binding site 6 out of 6 in the Prolyl Oligopeptidase Mutant S477C From Pyrococcus Furiosus


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Prolyl Oligopeptidase Mutant S477C From Pyrococcus Furiosus within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl703 b:58.3 occ:1.00 NH1 B:ARG476 3.0 47.9 1.0 O B:HOH1044 3.0 47.3 1.0 NH2 B:ARG476 3.1 42.0 1.0 OE1 B:GLU603 3.1 33.8 1.0 OH B:TYR501 3.4 41.0 1.0 NH1 B:ARG600 3.4 43.7 1.0 CZ B:ARG476 3.5 49.0 1.0 CZ B:TYR501 3.7 35.9 1.0 CE B:MET593 3.8 56.6 1.0 CZ B:ARG600 3.9 41.7 1.0 CE1 B:TYR501 4.0 39.2 1.0 CD B:GLU603 4.0 33.0 1.0 CD B:ARG600 4.1 36.3 1.0 OE2 B:GLU603 4.2 40.2 1.0 NE B:ARG600 4.2 35.6 1.0 CG B:MET593 4.2 61.7 1.0 CE2 B:TYR501 4.3 37.6 1.0 SD B:MET593 4.6 59.6 1.0 CB B:MET593 4.6 64.4 1.0 NH2 B:ARG600 4.7 40.4 1.0 NE B:ARG476 4.8 40.4 1.0 CD1 B:TYR501 4.9 35.8 1.0

K.Ellis-Guardiola, H.Rui, R.L.Beckner, P.Srivastava, N.Sukumar, B.Roux, J.C.Lewis. Crystal Structure and Conformational Dynamics of Pyrococcus Furiosus Prolyl Oligopeptidase. Biochemistry V. 58 1616 2019.
ISSN: ISSN 0006-2960
PubMed: 30786206
DOI: 10.1021/ACS.BIOCHEM.9B00031