Iron 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
Calcium	(Ca)	2 atoms

The binding sites of Iron 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 Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Native Human Myeloperoxidase in Complex with Cpd 9, PDB code: 7ni1:
Jump to Iron binding site number: 1; 2;

Iron 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 Iron with other atoms in the Fe 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 A:Fe203 b:20.1 occ:1.00 FE A:HEM203 0.0 20.1 1.0 NA A:HEM203 1.9 20.5 1.0 NB A:HEM203 2.0 19.9 1.0 ND A:HEM203 2.0 20.0 1.0 NC A:HEM203 2.0 20.0 1.0 NE2 C:HIS336 2.1 12.5 1.0 O A:HOH308 2.8 10.4 1.0 C1A A:HEM203 2.9 20.6 1.0 C4D A:HEM203 3.0 20.3 1.0 C4B A:HEM203 3.0 20.2 1.0 C4A A:HEM203 3.0 20.5 1.0 C1D A:HEM203 3.0 20.3 1.0 C1B A:HEM203 3.0 20.4 1.0 C1C A:HEM203 3.0 20.0 1.0 C4C A:HEM203 3.1 20.2 1.0 CE1 C:HIS336 3.1 12.1 1.0 CD2 C:HIS336 3.1 12.5 1.0 CHA A:HEM203 3.3 21.0 1.0 CHC A:HEM203 3.4 20.7 1.0 CHB A:HEM203 3.4 20.8 1.0 CHD A:HEM203 3.4 20.8 1.0 C2A A:HEM203 4.1 21.0 1.0 C3A A:HEM203 4.2 21.0 1.0 CG C:HIS336 4.3 10.2 1.0 ND1 C:HIS336 4.3 11.8 1.0 C3D A:HEM203 4.3 20.6 1.0 C2B A:HEM203 4.3 20.5 1.0 C2C A:HEM203 4.3 20.4 1.0 C3B A:HEM203 4.3 20.6 1.0 C3C A:HEM203 4.3 20.5 1.0 C2D A:HEM203 4.3 20.6 1.0 CD2 C:LEU417 4.7 14.1 1.0 O22 C:UEB606 4.8 18.2 1.0 CG C:ARG333 5.0 19.9 1.0

Iron 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 Iron with other atoms in the Fe 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 B:Fe203 b:22.8 occ:1.00 FE B:HEM203 0.0 22.8 1.0 NA B:HEM203 2.0 22.9 1.0 ND B:HEM203 2.0 22.7 1.0 NC B:HEM203 2.0 23.1 1.0 NB B:HEM203 2.0 22.6 1.0 NE2 D:HIS336 2.1 17.7 1.0 O B:HOH337 2.8 18.7 1.0 C4D B:HEM203 3.0 23.0 1.0 C1D B:HEM203 3.0 23.1 1.0 C1A B:HEM203 3.0 23.1 1.0 C4B B:HEM203 3.0 23.0 1.0 C1C B:HEM203 3.0 23.1 1.0 C4C B:HEM203 3.0 23.2 1.0 C1B B:HEM203 3.0 22.9 1.0 C4A B:HEM203 3.0 22.9 1.0 CD2 D:HIS336 3.1 18.1 1.0 CE1 D:HIS336 3.1 17.0 1.0 CHA B:HEM203 3.3 23.5 1.0 CHC B:HEM203 3.4 23.8 1.0 CHD B:HEM203 3.4 23.7 1.0 CHB B:HEM203 3.4 23.3 1.0 C2A B:HEM203 4.2 23.4 1.0 C3A B:HEM203 4.2 23.4 1.0 C2C B:HEM203 4.2 23.6 1.0 C3C B:HEM203 4.2 23.6 1.0 C3D B:HEM203 4.3 23.4 1.0 CG D:HIS336 4.3 16.5 1.0 C2D B:HEM203 4.3 23.3 1.0 ND1 D:HIS336 4.3 17.3 1.0 C3B B:HEM203 4.3 23.3 1.0 C2B B:HEM203 4.3 23.1 1.0 CD2 D:LEU417 4.7 17.2 1.0 O22 D:UEB606 4.9 22.4 1.0 CL B:CL202 4.9 21.7 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