Chlorine in PDB 7qzr: Structure of Native Leukocyte Myeloperoxidase in Complex with the Staphyloccal Peroxidase Inhibitor Spin From Staphylococcus Aureus

The structure of Structure of Native Leukocyte Myeloperoxidase in Complex with the Staphyloccal Peroxidase Inhibitor Spin From Staphylococcus Aureus, PDB code: 7qzr was solved by V.Pfanzagl, J.A.Brito, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.81 / 2.18
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	112.085, 112.085, 249.949, 90, 90, 90
R / Rfree (%)	20.4 / 24.4

The structure of Structure of Native Leukocyte Myeloperoxidase in Complex with the Staphyloccal Peroxidase Inhibitor Spin From Staphylococcus Aureus also contains other interesting chemical elements:

Iron	(Fe)	2 atoms
Calcium	(Ca)	2 atoms

The binding sites of Chlorine atom in the Structure of Native Leukocyte Myeloperoxidase in Complex with the Staphyloccal Peroxidase Inhibitor Spin From Staphylococcus Aureus (pdb code 7qzr). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of Native Leukocyte Myeloperoxidase in Complex with the Staphyloccal Peroxidase Inhibitor Spin From Staphylococcus Aureus, PDB code: 7qzr:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Structure of Native Leukocyte Myeloperoxidase in Complex with the Staphyloccal Peroxidase Inhibitor Spin From Staphylococcus Aureus


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Native Leukocyte Myeloperoxidase in Complex with the Staphyloccal Peroxidase Inhibitor Spin From Staphylococcus Aureus within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl303 b:21.5 occ:1.00 H A:TRP198 2.2 21.6 0.0 H B:VAL493 2.5 18.2 0.0 HA A:ARG197 2.6 22.7 0.0 HH2 B:TRP602 2.7 18.3 0.0 HB3 B:ASN492 2.9 19.5 0.0 HB B:VAL493 3.1 17.9 0.0 N A:TRP198 3.1 23.5 1.0 H A:LEU199 3.2 20.6 0.0 O A:HOH404 3.3 23.3 1.0 H B:ASN492 3.3 18.9 0.0 HB1 B:ALA491 3.4 19.7 0.0 N B:VAL493 3.4 21.4 1.0 HG12 B:VAL493 3.4 18.1 0.0 HG2 A:ARG197 3.5 26.5 0.0 CA A:ARG197 3.5 24.6 1.0 HZ2 B:TRP602 3.5 18.3 0.0 HB2 A:TRP198 3.6 20.4 0.0 CH2 B:TRP602 3.6 21.1 1.0 N B:ASN492 3.8 22.0 1.0 CB B:ASN492 3.8 22.7 1.0 HH11 A:ARG197 3.8 27.9 0.0 C A:ARG197 3.8 24.3 1.0 HD22 B:LEU596 3.8 20.0 0.0 CB B:VAL493 3.9 21.1 1.0 HB3 A:ARG197 4.0 24.3 0.0 HD21 B:LEU596 4.0 19.9 0.0 CG1 B:VAL493 4.0 21.2 1.0 CZ2 B:TRP602 4.0 21.2 1.0 HB2 B:ASN492 4.0 19.6 0.0 HG11 B:VAL493 4.1 18.2 0.0 CA B:ASN492 4.1 21.9 1.0 O A:VAL196 4.1 23.5 1.0 CB A:ARG197 4.1 25.9 1.0 CA A:TRP198 4.1 22.7 1.0 N A:LEU199 4.2 22.2 1.0 C B:ASN492 4.2 21.9 1.0 HD23 B:LEU596 4.2 20.1 0.0 CD2 B:LEU596 4.2 23.1 1.0 HD3 A:ARG197 4.2 29.3 0.0 CA B:VAL493 4.2 21.3 1.0 CG A:ARG197 4.3 28.4 1.0 CB A:TRP198 4.3 22.3 1.0 CB B:ALA491 4.4 22.7 1.0 C B:ALA491 4.5 22.9 1.0 O A:LEU199 4.5 23.4 1.0 HA B:ALA491 4.6 19.8 0.0 HA B:VAL493 4.7 17.9 0.0 C A:TRP198 4.7 22.3 1.0 NH1 A:ARG197 4.7 29.8 1.0 N A:ARG197 4.7 24.3 1.0 HB2 A:LEU199 4.7 21.0 0.0 CD A:ARG197 4.8 31.0 1.0 CZ3 B:TRP602 4.8 21.1 1.0 CA B:ALA491 4.8 22.8 1.0 HB3 B:ALA491 4.8 19.6 0.0 C A:VAL196 4.9 23.6 1.0 CG A:TRP198 4.9 22.3 1.0 HZ3 B:TRP602 5.0 18.5 0.0

Chlorine binding site 2 out of 2 in the Structure of Native Leukocyte Myeloperoxidase in Complex with the Staphyloccal Peroxidase Inhibitor Spin From Staphylococcus Aureus


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of Native Leukocyte Myeloperoxidase in Complex with the Staphyloccal Peroxidase Inhibitor Spin From Staphylococcus Aureus within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl302 b:20.9 occ:1.00 H C:TRP198 2.1 17.1 0.0 H D:VAL493 2.5 18.4 0.0 HA C:ARG197 2.6 18.7 0.0 HH2 D:TRP602 2.8 17.5 0.0 HB3 D:ASN492 2.9 18.1 0.0 O C:HOH420 3.1 25.7 1.0 N C:TRP198 3.1 20.8 1.0 H C:LEU199 3.1 15.6 0.0 H D:ASN492 3.2 17.0 0.0 HG2 C:ARG197 3.3 21.8 0.0 HB D:VAL493 3.3 19.4 0.0 HZ2 D:TRP602 3.4 17.5 0.0 HG12 D:VAL493 3.4 19.6 0.0 N D:VAL493 3.4 22.2 1.0 HB2 C:TRP198 3.5 17.0 0.0 CA C:ARG197 3.5 22.2 1.0 HB1 D:ALA491 3.6 16.7 0.0 CH2 D:TRP602 3.7 20.9 1.0 CB D:ASN492 3.7 21.8 1.0 HB2 D:ASN492 3.8 18.2 0.0 N D:ASN492 3.8 20.7 1.0 HD22 D:LEU596 3.8 22.4 0.0 HH11 C:ARG197 3.8 21.7 0.0 C C:ARG197 3.8 21.6 1.0 HB3 C:ARG197 3.9 20.2 0.0 CZ2 D:TRP602 3.9 20.9 1.0 CB D:VAL493 4.0 23.1 1.0 CB C:ARG197 4.1 23.4 1.0 N C:LEU199 4.1 19.1 1.0 CG1 D:VAL493 4.1 23.4 1.0 CA D:ASN492 4.1 21.2 1.0 CA C:TRP198 4.1 20.6 1.0 HD21 D:LEU596 4.1 22.3 0.0 CG C:ARG197 4.1 25.3 1.0 HG11 D:VAL493 4.2 19.7 0.0 HD23 D:LEU596 4.2 22.5 0.0 CD2 D:LEU596 4.2 26.0 1.0 C D:ASN492 4.2 21.9 1.0 O C:VAL196 4.3 23.7 1.0 CB C:TRP198 4.3 20.7 1.0 CA D:VAL493 4.3 22.4 1.0 O C:LEU199 4.4 19.3 1.0 HB2 C:LEU199 4.5 14.9 0.0 HD3 C:ARG197 4.6 24.6 0.0 C C:TRP198 4.6 19.9 1.0 CB D:ALA491 4.6 20.4 1.0 NH1 C:ARG197 4.6 25.3 1.0 C D:ALA491 4.6 20.5 1.0 N C:ARG197 4.7 22.5 1.0 HA D:VAL493 4.8 18.5 0.0 HA D:ALA491 4.8 16.6 0.0 CZ3 D:TRP602 4.8 20.9 1.0 CG C:TRP198 4.9 21.6 1.0 HG3 C:ARG197 4.9 22.1 0.0 HH12 C:ARG197 4.9 21.6 0.0 CD C:ARG197 4.9 27.8 1.0 C C:VAL196 4.9 23.2 1.0 CA D:ALA491 5.0 20.3 1.0 CG D:ASN492 5.0 24.5 1.0

U.Leitgeb, P.G.Furtmuller, S.Hofbauer, J.A.Brito, C.Obinger, V.Pfanzagl. The Staphylococcal Inhibitory Protein Spin Binds to Human Myeloperoxidase with Picomolar Affinity But Only Dampens Halide Oxidation. J.Biol.Chem. V. 298 02514 2022.
ISSN: ESSN 1083-351X
PubMed: 36150500
DOI: 10.1016/J.JBC.2022.102514