Calcium in PDB 7ni1: Crystal Structure of Native Human Myeloperoxidase in Complex with Cpd 9

All present enzymatic activity of Crystal Structure of Native Human Myeloperoxidase in Complex with Cpd 9:
1.11.2.2;

The structure of Crystal Structure of Native Human Myeloperoxidase in Complex with Cpd 9, PDB code: 7ni1 was solved by T.Sjogren, T.Inghardt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.24 / 2.11
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	93.22, 63.82, 111.34, 90, 97.24, 90
R / Rfree (%)	21.7 / 25.6

The structure of Crystal Structure of Native Human Myeloperoxidase in Complex with Cpd 9 also contains other interesting chemical elements:

Chlorine	(Cl)	7 atoms
Iron	(Fe)	2 atoms

The binding sites of Calcium atom in the Crystal Structure of Native Human Myeloperoxidase in Complex with Cpd 9 (pdb code 7ni1). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Native Human Myeloperoxidase in Complex with Cpd 9, PDB code: 7ni1:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Native Human Myeloperoxidase in Complex with Cpd 9


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Native Human Myeloperoxidase in Complex with Cpd 9 within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca601 b:13.0 occ:0.96 O A:ASP96 2.2 15.5 1.0 O C:THR168 2.3 14.2 1.0 OG1 C:THR168 2.3 15.8 1.0 O C:PHE170 2.3 13.4 1.0 OG C:SER174 2.4 25.9 1.0 OD1 C:ASP172 2.6 15.9 1.0 OD1 A:ASP96 2.7 17.2 1.0 C C:THR168 3.2 14.8 1.0 C A:ASP96 3.4 14.0 1.0 CB C:SER174 3.4 15.2 1.0 C C:PHE170 3.5 12.9 1.0 CG C:ASP172 3.5 17.8 1.0 CB C:THR168 3.6 14.8 1.0 CG A:ASP96 3.8 16.2 1.0 CA C:THR168 3.8 8.5 1.0 N C:PHE170 3.9 9.0 1.0 OD2 C:ASP172 3.9 21.7 1.0 C C:SER169 4.1 14.3 1.0 N C:THR168 4.1 8.8 1.0 CA A:ASP96 4.1 9.3 1.0 CA C:PHE170 4.1 9.3 1.0 N C:SER169 4.2 13.3 1.0 N C:SER174 4.2 13.1 1.0 N C:ASP172 4.3 10.3 1.0 O C:SER169 4.4 12.9 1.0 CB A:ASP96 4.4 10.8 1.0 CA C:SER174 4.4 11.9 1.0 N A:LEU97 4.4 11.4 1.0 O C:HOH754 4.5 8.5 1.0 CA C:SER169 4.5 12.3 1.0 N C:VAL171 4.6 9.9 1.0 CA A:LEU97 4.6 10.2 1.0 CG2 C:THR168 4.7 13.6 1.0 CB C:PHE170 4.7 10.1 1.0 CB C:ASP172 4.7 12.8 1.0 OD2 A:ASP96 4.7 19.7 1.0 CA C:VAL171 4.9 7.4 1.0 CA C:ASP172 5.0 11.5 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Native Human Myeloperoxidase in Complex with Cpd 9


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Native Human Myeloperoxidase in Complex with Cpd 9 within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca605 b:10.6 occ:0.81 O B:ASP96 2.2 17.1 1.0 O D:PHE170 2.3 12.4 1.0 OD1 B:ASP96 2.3 24.9 1.0 OG D:SER174 2.4 24.1 1.0 O D:THR168 2.4 12.2 1.0 OG1 D:THR168 2.6 18.1 1.0 OD1 D:ASP172 2.6 19.5 1.0 C B:ASP96 3.3 16.7 1.0 C D:THR168 3.4 13.3 1.0 CB D:SER174 3.4 16.0 1.0 CG B:ASP96 3.5 23.5 1.0 C D:PHE170 3.5 13.2 1.0 CG D:ASP172 3.6 21.3 1.0 CB D:THR168 3.8 14.7 1.0 CA B:ASP96 4.0 13.9 1.0 N D:PHE170 4.0 10.6 1.0 OD2 D:ASP172 4.0 22.5 1.0 CA D:THR168 4.0 8.8 1.0 N D:SER174 4.1 16.0 1.0 C D:SER169 4.1 14.2 1.0 N D:ASP172 4.2 15.9 1.0 CA D:PHE170 4.2 9.6 1.0 CB B:ASP96 4.2 14.9 1.0 N D:THR168 4.2 8.2 1.0 N B:LEU97 4.3 14.5 1.0 CA D:SER174 4.4 14.2 1.0 OD2 B:ASP96 4.4 18.8 1.0 N D:SER169 4.4 10.9 1.0 O D:SER169 4.4 15.4 1.0 N D:VAL171 4.6 11.7 1.0 O B:HOH308 4.6 14.4 1.0 CA B:LEU97 4.6 14.7 1.0 CA D:SER169 4.7 11.1 1.0 CB D:ASP172 4.7 18.5 1.0 CA D:VAL171 4.8 12.1 1.0 CB D:PHE170 4.8 10.9 1.0 CG2 D:THR168 4.9 11.9 1.0 CA D:ASP172 4.9 16.7 1.0 N D:ALA173 4.9 17.0 1.0

T.Inghardt, T.Antonsson, C.Ericsson, D.Hovdal, P.Johannesson, C.Johansson, U.Jurva, J.Kajanus, B.Kull, E.Michaelsson, A.Pettersen, T.Sjogren, H.Sorensen, K.Westerlund, E.L.Lindstedt. Discovery of AZD4831, A Mechanism-Based Irreversible Inhibitor of Myeloperoxidase, As A Potential Treatment For Heart Failure with Preserved Ejection Fraction. J.Med.Chem. V. 65 11485 2022.
ISSN: ISSN 0022-2623
PubMed: 36005476
DOI: 10.1021/ACS.JMEDCHEM.1C02141