Chlorine in PDB 4ov8: Crystal Structure of the TMH1-Lock Mutant of the Mature Form of Pleurotolysin B

The structure of Crystal Structure of the TMH1-Lock Mutant of the Mature Form of Pleurotolysin B, PDB code: 4ov8 was solved by S.C.Kondos, R.H.P.Law, J.C.Whisstock, M.A.Dunstone, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	61.64 / 2.15
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	71.181, 71.181, 174.675, 90.00, 90.00, 120.00
R / Rfree (%)	20.7 / 24.3

The binding sites of Chlorine atom in the Crystal Structure of the TMH1-Lock Mutant of the Mature Form of Pleurotolysin B (pdb code 4ov8). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 6 binding sites of Chlorine where determined in the Crystal Structure of the TMH1-Lock Mutant of the Mature Form of Pleurotolysin B, PDB code: 4ov8:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6;

Chlorine binding site 1 out of 6 in the Crystal Structure of the TMH1-Lock Mutant of the Mature Form of Pleurotolysin B


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 the TMH1-Lock Mutant of the Mature Form of Pleurotolysin B within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl603 b:81.1 occ:1.00 OE1 A:GLU124 3.7 66.6 1.0 O A:THR121 4.2 43.3 1.0 OG A:SER125 4.3 36.1 1.0 CB A:GLU124 4.3 31.4 1.0 CB A:THR121 4.5 36.1 1.0 CA A:THR121 4.6 35.7 1.0 CG2 A:THR121 4.8 45.9 1.0 CD A:GLU124 4.8 62.9 1.0 C A:THR121 4.9 46.0 1.0 O A:ASP83 4.9 81.2 1.0

Chlorine binding site 2 out of 6 in the Crystal Structure of the TMH1-Lock Mutant of the Mature Form of Pleurotolysin B


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 the TMH1-Lock Mutant of the Mature Form of Pleurotolysin B within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl605 b:68.1 occ:1.00 N A:GLY296 3.6 48.5 1.0 CG A:ARG319 3.9 49.7 1.0 CA A:ASN295 4.0 48.8 1.0 ND2 A:ASN295 4.1 51.1 1.0 C A:ASN295 4.4 54.8 1.0 CB A:ASN295 4.4 45.2 1.0 CB A:ARG319 4.6 47.1 1.0 O A:VAL294 4.6 50.0 1.0 CA A:GLY296 4.6 52.3 1.0 CD A:ARG319 4.6 57.2 1.0 NE A:ARG319 4.6 54.2 1.0 CG A:ASN295 4.8 46.9 1.0

Chlorine binding site 3 out of 6 in the Crystal Structure of the TMH1-Lock Mutant of the Mature Form of Pleurotolysin B


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of the TMH1-Lock Mutant of the Mature Form of Pleurotolysin B within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl606 b:88.2 occ:1.00 O A:HOH830 2.5 64.9 1.0 N A:SER415 3.1 84.8 1.0 OG A:SER415 3.3 85.0 1.0 CA A:GLY414 3.5 83.9 1.0 C A:GLY414 3.8 90.4 1.0 CB A:SER415 3.9 82.4 1.0 CA A:SER415 4.1 83.6 1.0 CD2 A:PHE422 4.3 57.9 1.0 CE2 A:PHE422 4.3 60.4 1.0 CG A:PHE422 4.4 57.8 1.0 CZ A:PHE422 4.5 63.3 1.0 CD1 A:PHE422 4.5 59.5 1.0 CE1 A:PHE422 4.5 61.2 1.0 NE2 A:HIS412 4.7 54.3 1.0 N A:GLY414 4.8 80.0 1.0 O A:GLN413 4.8 56.7 1.0 N A:GLY416 4.8 97.5 1.0 CD2 A:HIS412 5.0 58.7 1.0

Chlorine binding site 4 out of 6 in the Crystal Structure of the TMH1-Lock Mutant of the Mature Form of Pleurotolysin B


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of the TMH1-Lock Mutant of the Mature Form of Pleurotolysin B within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl607 b:0.8 occ:1.00 O A:HOH853 2.4 38.2 1.0 NH1 A:ARG508 2.7 39.5 1.0 CZ A:ARG508 3.3 44.5 1.0 CD A:ARG508 3.3 32.4 1.0 O A:GLY459 3.5 31.8 1.0 NE A:ARG508 3.5 32.3 1.0 CA A:ARG460 3.9 44.8 1.0 NH2 A:ARG508 4.2 34.5 1.0 CB A:ARG460 4.3 33.3 1.0 O A:HOH840 4.4 37.9 1.0 CG A:ARG508 4.4 37.5 1.0 C A:GLY459 4.5 40.9 1.0 N A:TYR461 4.5 38.5 1.0 N A:ARG460 4.7 33.0 1.0 C A:ARG460 4.8 34.9 1.0

Chlorine binding site 5 out of 6 in the Crystal Structure of the TMH1-Lock Mutant of the Mature Form of Pleurotolysin B


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Crystal Structure of the TMH1-Lock Mutant of the Mature Form of Pleurotolysin B within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl608 b:87.7 occ:1.00 O A:PRO505 3.7 68.3 1.0 CE1 A:TYR430 3.9 53.1 1.0 N A:TYR430 3.9 35.4 1.0 OE1 A:GLN429 4.0 58.1 1.0 CD1 A:TYR430 4.0 43.1 1.0 CZ A:TYR430 4.0 58.0 1.0 CG A:TYR430 4.2 54.7 1.0 CE2 A:TYR430 4.2 46.8 1.0 O A:TYR430 4.3 39.8 1.0 CD2 A:TYR430 4.3 49.9 1.0 O A:HOH738 4.4 38.9 1.0 CD A:GLN429 4.5 55.9 1.0 OH A:TYR430 4.6 62.2 1.0 CA A:GLN429 4.6 37.5 1.0 CB A:PRO507 4.7 41.1 1.0 C A:PRO505 4.7 69.3 1.0 CA A:TYR430 4.8 44.5 1.0 C A:GLN429 4.8 37.9 1.0 NE2 A:GLN429 4.8 64.8 1.0 N A:PRO507 4.8 50.4 1.0 CD A:PRO507 4.8 45.2 1.0 CA A:PRO507 4.8 46.4 1.0 C A:TYR430 4.9 37.3 1.0 O A:TYR428 4.9 30.4 1.0

Chlorine binding site 6 out of 6 in the Crystal Structure of the TMH1-Lock Mutant of the Mature Form of Pleurotolysin B


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Crystal Structure of the TMH1-Lock Mutant of the Mature Form of Pleurotolysin B within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl609 b:76.8 occ:1.00 O A:HOH855 2.4 56.8 1.0 O A:ASP184 3.1 0.3 1.0 O A:ASP174 3.5 78.5 1.0 N A:THR176 3.9 60.5 1.0 CA A:PHE175 4.0 71.1 1.0 C A:ASP184 4.1 0.0 1.0 OG1 A:THR176 4.2 80.1 1.0 N A:ARG100 4.2 76.8 1.0 CB A:ASP184 4.3 0.6 1.0 CB A:ARG100 4.3 72.7 1.0 C A:ASP174 4.5 72.9 1.0 C A:PHE175 4.5 70.5 1.0 CD2 A:PHE175 4.5 68.1 1.0 CA A:ASP184 4.5 0.5 1.0 CG2 A:ILE186 4.7 84.3 1.0 N A:PHE175 4.7 63.0 1.0 CB A:THR176 4.8 72.5 1.0 CB A:PHE175 4.8 60.9 1.0 CA A:ARG100 4.9 77.8 1.0 CA A:THR176 4.9 59.0 1.0 CG A:PHE175 4.9 51.2 1.0 O A:THR98 4.9 92.9 1.0

N.Lukoyanova, S.C.Kondos, I.Farabella, R.H.P.Law, C.F.Reboul, T.T.Caradoc-Davies, B.A.Spicer, O.Kleifeld, D.A.Traore, S.M.Ekkel, I.Voskoboinik, J.A.Trapani, T.Hatfaludi, K.Oliver, E.M.Hotze, R.K.Tweten, J.C.Whisstock, M.Topf, H.R.Saibil, M.A.Dunstone. Conformational Changes During Pore Formation By the Perforin-Related Protein Pleurotolysin Plos Biol. V. 13 02049 2015.
ISSN: ISSN 1544-9173
PubMed: 25654333
DOI: 10.1371/JOURNAL.PBIO.1002049