Chlorine in PDB 7oih: Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase

All present enzymatic activity of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase:
1.11.2.2;

The structure of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase, PDB code: 7oih was solved by L.Krawczyk, S.Semwal, J.Bouckaert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.99 / 2.60
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	155.91, 144.634, 236.454, 90, 91.53, 90
R / Rfree (%)	17.9 / 22

The structure of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase also contains other interesting chemical elements:

Iron	(Fe)	8 atoms
Calcium	(Ca)	8 atoms
Fluorine	(F)	4 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30; Page 4, Binding sites: 31 - 36;

Binding sites:

The binding sites of Chlorine atom in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase (pdb code 7oih). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 36 binding sites of Chlorine where determined in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase, PDB code: 7oih:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Chlorine binding site 1 out of 36 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl801 b:43.3 occ:1.00 O A:HOH1033 3.0 29.4 1.0 N A:TRP198 3.2 42.1 1.0 N A:VAL493 3.4 38.9 1.0 CH2 A:TRP602 3.6 32.3 1.0 CB A:ASN492 3.7 46.3 1.0 CA A:ARG197 3.8 46.0 1.0 CB A:VAL493 3.8 39.3 1.0 CZ2 A:TRP602 3.9 35.6 1.0 N A:ASN492 3.9 45.6 1.0 CG1 A:VAL493 3.9 36.4 1.0 C A:ARG197 4.0 41.7 1.0 N A:LEU199 4.1 43.2 1.0 CA A:ASN492 4.1 47.3 1.0 CD2 A:LEU596 4.1 42.0 1.0 CB A:TRP198 4.2 39.8 1.0 CA A:VAL493 4.2 37.3 1.0 CA A:TRP198 4.2 41.0 1.0 O A:VAL196 4.2 40.1 1.0 C A:ASN492 4.2 44.5 1.0 CD A:ARG197 4.4 44.2 1.0 CB A:ARG197 4.5 47.4 1.0 O A:LEU199 4.6 40.0 1.0 CB A:ALA491 4.6 39.6 1.0 C A:TRP198 4.7 44.0 1.0 C A:ALA491 4.7 42.0 1.0 CZ3 A:TRP602 4.8 35.5 1.0 CG A:TRP198 4.8 40.4 1.0 N A:ARG197 4.8 48.8 1.0 CG A:ARG197 4.8 48.0 1.0 NH1 A:ARG197 4.9 40.5 1.0 C A:VAL196 5.0 47.4 1.0 CG A:ASN492 5.0 42.3 1.0

Chlorine binding site 2 out of 36 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl802 b:77.2 occ:1.00 N A:THR710 3.5 70.6 1.0 NE A:ARG548 3.6 64.2 1.0 O A:ASN514 3.6 78.9 1.0 OG1 A:THR710 3.9 60.1 1.0 N A:THR711 3.9 58.2 1.0 NH2 A:ARG548 3.9 63.6 1.0 CB A:ASN514 3.9 82.2 1.0 CA A:ILE709 3.9 67.9 1.0 CA A:ASN514 3.9 79.0 1.0 CG2 A:ILE709 4.1 63.2 1.0 CZ A:ARG548 4.2 59.0 1.0 CE1 A:TYR516 4.2 63.8 1.0 C A:ILE709 4.2 69.3 1.0 C A:ASN514 4.2 72.8 1.0 CB A:ILE709 4.4 65.3 1.0 CA A:THR710 4.4 66.0 1.0 O A:THR711 4.6 68.0 1.0 O A:GLY708 4.6 60.1 1.0 CD A:ARG548 4.6 58.5 1.0 CB A:THR711 4.6 59.3 1.0 C A:THR710 4.6 57.5 1.0 OG1 A:THR711 4.7 68.0 1.0 CA A:THR711 4.7 58.9 1.0 CB A:THR710 4.8 61.2 1.0 CG1 A:ILE709 4.8 73.6 1.0 CD1 A:TYR516 4.8 59.3 1.0

Chlorine binding site 3 out of 36 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl803 b:51.5 occ:1.00 N A:GLN367 3.4 51.4 1.0 N A:PHE379 3.6 45.4 1.0 OD1 A:ASN366 3.7 60.5 1.0 CG A:ASN366 3.9 57.1 1.0 CA A:ASN366 3.9 51.5 1.0 CD2 A:PHE379 4.1 41.4 1.0 ND2 A:ASN366 4.1 54.5 1.0 CA A:PRO378 4.2 47.0 1.0 C A:ASN366 4.2 52.5 1.0 CB A:PHE379 4.2 45.6 1.0 CB A:GLN367 4.2 53.7 1.0 CA A:GLN367 4.3 52.4 1.0 C A:PRO378 4.4 46.3 1.0 CG A:GLN367 4.4 57.0 1.0 CG A:PHE379 4.4 43.5 1.0 CA A:PHE379 4.5 48.3 1.0 CB A:ASN366 4.5 56.8 1.0 CB A:PRO378 4.6 45.5 1.0 N A:ARG368 4.6 57.7 1.0 O A:VAL365 4.7 41.2 1.0 C A:GLN367 4.9 53.6 1.0 CE2 A:PHE379 5.0 37.4 1.0 O A:PHE379 5.0 48.7 1.0 N A:ASN366 5.0 47.4 1.0

Chlorine binding site 4 out of 36 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl808 b:62.7 occ:1.00 ND2 A:ASN623 3.4 55.5 1.0 CB A:ASN561 3.9 49.3 1.0 OD1 A:ASN623 4.0 42.7 1.0 CG A:ASN623 4.1 49.6 1.0 CB A:LEU626 4.2 48.9 1.0 O A:GLN560 4.3 58.4 1.0 CD A:LYS625 4.3 85.0 1.0 N A:LEU626 4.3 58.8 1.0 C A:GLN560 4.5 53.6 1.0 NZ A:LYS629 4.5 84.8 1.0 CB A:LYS625 4.5 78.3 1.0 CA A:ASN561 4.5 49.2 1.0 CE A:LYS629 4.5 76.6 1.0 CA A:LEU626 4.6 52.9 1.0 N A:ASN561 4.6 52.7 1.0 CG A:LYS625 4.6 80.8 1.0 CB A:GLN560 4.8 51.3 1.0 CG A:ASN561 4.8 53.8 1.0 CE A:LYS625 5.0 92.2 1.0

Chlorine binding site 5 out of 36 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl809 b:51.2 occ:1.00 NE1 A:TRP680 3.5 48.5 1.0 CZ2 A:TRP680 3.8 49.9 1.0 CB A:TYR459 4.0 40.6 1.0 CE2 A:TRP680 4.0 50.6 1.0 CA A:ILE456 4.0 39.2 1.0 O A:HOH903 4.2 63.1 1.0 N A:ARG460 4.3 46.5 1.0 CZ2 A:TRP679 4.3 45.5 1.0 CG1 A:ILE456 4.4 39.5 1.0 O A:ILE456 4.4 36.5 1.0 CB A:ARG460 4.5 46.1 1.0 O A:GLN455 4.5 37.8 1.0 CB A:ILE456 4.6 40.0 1.0 C A:TYR459 4.6 39.1 1.0 OE1 A:GLU681 4.6 56.8 1.0 CD1 A:TRP680 4.7 46.1 1.0 CH2 A:TRP679 4.7 46.1 1.0 C A:ILE456 4.7 40.6 1.0 CA A:ARG460 4.7 45.7 1.0 CG2 A:ILE456 4.8 43.7 1.0 CA A:TYR459 4.8 38.2 1.0 N A:ILE456 4.8 41.5 1.0 C A:GLN455 4.9 41.5 1.0 CD A:GLU681 5.0 62.1 1.0

Chlorine binding site 6 out of 36 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl801 b:50.7 occ:1.00 O B:HOH1011 2.7 33.1 1.0 N B:TRP198 3.2 40.9 1.0 N B:VAL493 3.5 44.6 1.0 CA B:ARG197 3.6 39.0 1.0 CH2 B:TRP602 3.6 46.1 1.0 CB B:ASN492 3.7 34.7 1.0 N B:ASN492 3.8 37.0 1.0 C B:ARG197 3.9 40.4 1.0 CB B:VAL493 3.9 39.4 1.0 CZ2 B:TRP602 4.0 39.1 1.0 O B:VAL196 4.0 39.0 1.0 CG1 B:VAL493 4.0 37.2 1.0 CA B:ASN492 4.1 36.0 1.0 N B:LEU199 4.1 39.0 1.0 CA B:TRP198 4.2 38.7 1.0 C B:ASN492 4.2 39.0 1.0 CA B:VAL493 4.3 42.7 1.0 CD2 B:LEU596 4.3 38.1 1.0 CB B:TRP198 4.3 39.6 1.0 CB B:ARG197 4.3 41.1 1.0 CD B:ARG197 4.4 45.7 1.0 O B:LEU199 4.5 45.1 1.0 CB B:ALA491 4.5 46.9 1.0 C B:ALA491 4.6 36.8 1.0 N B:ARG197 4.7 45.2 1.0 C B:TRP198 4.7 40.8 1.0 NH1 B:ARG197 4.8 38.5 1.0 CG B:ARG197 4.8 44.0 1.0 C B:VAL196 4.8 45.4 1.0 CZ3 B:TRP602 4.8 43.5 1.0 CG B:TRP198 4.9 37.8 1.0 CG B:ASN492 4.9 36.9 1.0 CA B:ALA491 4.9 40.7 1.0

Chlorine binding site 7 out of 36 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 7 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl802 b:54.3 occ:1.00 NE1 B:TRP680 3.5 51.4 1.0 CZ2 B:TRP680 3.9 62.2 1.0 O B:HOH901 3.9 53.4 1.0 CB B:TYR459 3.9 46.9 1.0 CA B:ILE456 4.0 45.5 1.0 CE2 B:TRP680 4.0 57.8 1.0 N B:ARG460 4.1 49.2 1.0 CZ2 B:TRP679 4.3 40.3 1.0 CB B:ARG460 4.3 50.2 1.0 O B:ILE456 4.4 47.5 1.0 CG1 B:ILE456 4.4 54.9 1.0 O B:GLN455 4.5 49.8 1.0 C B:TYR459 4.5 48.0 1.0 CB B:ILE456 4.6 47.5 1.0 CA B:ARG460 4.6 48.3 1.0 OE1 B:GLU681 4.7 60.0 1.0 O B:HOH1175 4.7 51.6 1.0 CH2 B:TRP679 4.7 41.7 1.0 CA B:TYR459 4.7 44.5 1.0 C B:ILE456 4.7 46.4 1.0 CD1 B:TRP680 4.7 55.9 1.0 CG2 B:ILE456 4.8 50.1 1.0 N B:ILE456 4.8 49.4 1.0 C B:GLN455 4.9 47.0 1.0 CG B:TYR459 5.0 51.9 1.0

Chlorine binding site 8 out of 36 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 8 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl803 b:51.0 occ:0.81 N B:GLN367 3.4 60.8 1.0 N B:PHE379 3.7 52.0 1.0 OD1 B:ASN366 3.7 51.5 1.0 CG B:ASN366 3.9 51.4 1.0 CA B:ASN366 4.0 55.3 1.0 CD2 B:PHE379 4.2 69.6 1.0 C B:ASN366 4.2 59.0 1.0 ND2 B:ASN366 4.2 53.4 1.0 CA B:PRO378 4.3 49.3 1.0 CB B:GLN367 4.3 59.2 1.0 CA B:GLN367 4.3 59.4 1.0 CB B:PHE379 4.3 55.0 1.0 C B:PRO378 4.5 48.8 1.0 N B:ARG368 4.5 60.4 1.0 CB B:ASN366 4.6 50.5 1.0 CG B:PHE379 4.6 64.1 1.0 CA B:PHE379 4.6 54.8 1.0 CB B:PRO378 4.7 48.5 1.0 CG B:GLN367 4.8 67.3 1.0 C B:GLN367 4.8 59.2 1.0 O B:VAL365 4.8 53.7 1.0

Chlorine binding site 9 out of 36 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 9 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl810 b:78.1 occ:1.00 NH1 F:ARG653 4.4 53.3 1.0 O F:HOH1141 4.4 42.0 1.0 CA B:MET577 4.6 57.9 1.0 O B:VAL576 4.6 48.8 1.0 C B:MET577 4.7 58.0 1.0 CD1 B:LEU389 4.7 60.9 1.0 C B:VAL576 4.8 50.5 1.0 N B:MET577 4.9 54.7 1.0 O B:MET577 4.9 59.6 1.0 NH2 B:ARG392 4.9 91.9 1.0

Chlorine binding site 10 out of 36 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 10 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl811 b:60.0 occ:1.00 ND2 B:ASN623 3.7 42.8 1.0 CB B:ASN561 3.9 63.2 1.0 CB B:LEU626 3.9 57.1 1.0 O B:GLN560 4.0 41.3 1.0 N B:LEU626 4.1 56.7 1.0 CE B:LYS629 4.2 65.5 1.0 CA B:LEU626 4.2 51.8 1.0 OD1 B:ASN623 4.2 47.7 1.0 C B:GLN560 4.3 46.0 1.0 CA B:ASN561 4.4 59.0 1.0 CD B:LYS625 4.4 88.8 1.0 CG B:ASN623 4.4 43.9 1.0 CB B:LYS625 4.4 67.0 1.0 N B:ASN561 4.5 50.5 1.0 CG B:LYS625 4.5 81.2 1.0 CD B:LYS629 4.5 62.7 1.0 CD1 B:LEU626 4.6 54.7 1.0 C B:LYS625 4.7 58.9 1.0 CG B:LEU626 4.8 59.9 1.0 CB B:GLN560 4.9 42.6 1.0 CE B:LYS625 4.9 97.0 1.0 CG B:ASN561 5.0 60.8 1.0

L.Krawczyk, S.Semwal, J.Soubhye, S.Lemri Ouadriri, M.Prevost, P.Van Antwerpen, G.Roos, J.Bouckaert. Native Glycosylation and Binding of the Antidepressant Paroxetine in A Low-Resolution Crystal Structure of Human Myeloperoxidase. Acta Crystallogr D Struct V. 78 1099 2022BIOL.
ISSN: ISSN 2059-7983
PubMed: 36048150
DOI: 10.1107/S2059798322007082