Iron in PDB 7lae: Crystal Structure of Myeloperoxidase Subform C (Mpo) Complex with Compound-4

All present enzymatic activity of Crystal Structure of Myeloperoxidase Subform C (Mpo) Complex with Compound-4:
1.11.2.2;

The structure of Crystal Structure of Myeloperoxidase Subform C (Mpo) Complex with Compound-4, PDB code: 7lae was solved by J.A.Khan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.28 / 2.97
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	106.917, 106.917, 238.964, 90, 90, 90
R / Rfree (%)	21.6 / 26.7

The structure of Crystal Structure of Myeloperoxidase Subform C (Mpo) Complex with Compound-4 also contains other interesting chemical elements:

Chlorine	(Cl)	2 atoms
Calcium	(Ca)	2 atoms
Fluorine	(F)	2 atoms

The binding sites of Iron atom in the Crystal Structure of Myeloperoxidase Subform C (Mpo) Complex with Compound-4 (pdb code 7lae). 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 Myeloperoxidase Subform C (Mpo) Complex with Compound-4, PDB code: 7lae:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Myeloperoxidase Subform C (Mpo) Complex with Compound-4


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 Myeloperoxidase Subform C (Mpo) Complex with Compound-4 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe601 b:70.8 occ:1.00 FE B:HEM601 0.0 70.8 1.0 NB B:HEM601 1.9 70.5 1.0 NC B:HEM601 2.0 70.7 1.0 ND B:HEM601 2.0 70.9 1.0 NA B:HEM601 2.0 71.0 1.0 NE2 B:HIS336 2.2 66.0 1.0 C4B B:HEM601 2.9 70.8 1.0 C4D B:HEM601 2.9 71.2 1.0 C1B B:HEM601 3.0 70.9 1.0 C1D B:HEM601 3.0 71.2 1.0 C1C B:HEM601 3.0 70.7 1.0 C4C B:HEM601 3.0 71.0 1.0 C1A B:HEM601 3.0 71.2 1.0 C4A B:HEM601 3.1 71.0 1.0 CE1 B:HIS336 3.1 66.0 1.0 CD2 B:HIS336 3.3 66.0 1.0 CHA B:HEM601 3.4 71.6 1.0 CHC B:HEM601 3.4 71.3 1.0 CHD B:HEM601 3.4 71.7 1.0 CHB B:HEM601 3.4 71.3 1.0 C3B B:HEM601 4.2 71.2 1.0 N5 B:XRV611 4.2 65.1 1.0 N6 B:XRV611 4.2 66.6 1.0 C2B B:HEM601 4.2 71.0 1.0 C3D B:HEM601 4.2 71.7 1.0 C2D B:HEM601 4.2 71.5 1.0 C2C B:HEM601 4.2 71.3 1.0 C2A B:HEM601 4.2 71.5 1.0 C3C B:HEM601 4.2 71.3 1.0 C3A B:HEM601 4.3 71.5 1.0 ND1 B:HIS336 4.3 66.7 1.0 CG B:HIS336 4.3 64.3 1.0 CD2 B:LEU417 4.4 71.7 1.0 N4 B:XRV611 4.8 64.3 1.0 C3 B:XRV611 4.9 65.1 1.0 CD1 B:LEU417 4.9 69.4 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Myeloperoxidase Subform C (Mpo) Complex with Compound-4


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 Myeloperoxidase Subform C (Mpo) Complex with Compound-4 within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe604 b:47.4 occ:1.00 FE E:HEM604 0.0 47.4 1.0 NA E:HEM604 1.9 47.6 1.0 NB E:HEM604 2.0 47.1 1.0 ND E:HEM604 2.0 47.5 1.0 NC E:HEM604 2.0 47.3 1.0 NE2 E:HIS336 2.2 43.5 1.0 C4B E:HEM604 2.9 47.5 1.0 C4D E:HEM604 2.9 47.8 1.0 C1A E:HEM604 3.0 47.8 1.0 CE1 E:HIS336 3.0 43.0 1.0 C1B E:HEM604 3.0 47.6 1.0 C1D E:HEM604 3.0 47.8 1.0 C4A E:HEM604 3.0 47.5 1.0 C1C E:HEM604 3.0 47.2 1.0 C4C E:HEM604 3.0 47.5 1.0 CD2 E:HIS336 3.3 43.7 1.0 CHA E:HEM604 3.3 48.2 1.0 CHC E:HEM604 3.4 47.9 1.0 CHB E:HEM604 3.4 48.0 1.0 CHD E:HEM604 3.5 48.2 1.0 N6 E:XRV610 3.6 64.8 1.0 N5 E:XRV610 3.8 64.1 1.0 C3B E:HEM604 4.2 48.0 1.0 C2A E:HEM604 4.2 48.2 1.0 ND1 E:HIS336 4.2 43.0 1.0 C3A E:HEM604 4.2 48.0 1.0 C3D E:HEM604 4.2 48.3 1.0 C2B E:HEM604 4.2 47.8 1.0 C2D E:HEM604 4.2 48.2 1.0 C2C E:HEM604 4.2 47.8 1.0 C3C E:HEM604 4.2 47.8 1.0 CG E:HIS336 4.3 42.3 1.0 CD2 E:LEU417 4.5 64.8 1.0 C3 E:XRV610 4.5 63.8 1.0 N4 E:XRV610 4.7 62.0 1.0 CD1 E:LEU417 4.8 61.7 1.0 CG E:ARG333 4.9 41.8 1.0

C.H.Hu, M.W.Neissel Valente, O.Scott Halpern, S.Jusuf, J.A.Khan, G.A.Locke, G.J.Duke, X.Liu, F.J.Duclos, R.R.Wexler, E.K.Kick, J.M.Smallheer. Small Molecule and Macrocyclic Pyrazole Derived Inhibitors of Myeloperoxidase (Mpo). Bioorg.Med.Chem.Lett. 28010 2021.
ISSN: ESSN 1464-3405
PubMed: 33811992
DOI: 10.1016/J.BMCL.2021.128010