Iron in PDB 5mfa: Crystal Structure of Human Promyeloperoxidase (Prompo)

All present enzymatic activity of Crystal Structure of Human Promyeloperoxidase (Prompo):
1.11.2.2;

The structure of Crystal Structure of Human Promyeloperoxidase (Prompo), PDB code: 5mfa was solved by I.Grishkovskaya, P.G.Furtmueller, C.Obinger, K.Djinovic-Carugo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.68 / 1.20
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	106.152, 109.151, 83.961, 90.00, 122.66, 90.00
R / Rfree (%)	12.3 / 14.3

The structure of Crystal Structure of Human Promyeloperoxidase (Prompo) also contains other interesting chemical elements:

Calcium	(Ca)	1 atom
Chlorine	(Cl)	5 atoms

The binding sites of Iron atom in the Crystal Structure of Human Promyeloperoxidase (Prompo) (pdb code 5mfa). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of Human Promyeloperoxidase (Prompo), PDB code: 5mfa:

Iron binding site 1 out of 1 in the Crystal Structure of Human Promyeloperoxidase (Prompo)


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 Human Promyeloperoxidase (Prompo) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe812 b:11.6 occ:1.00 FE A:HEM812 0.0 11.6 1.0 NE2 A:HIS502 2.1 10.0 1.0 ND A:HEM812 2.1 10.8 1.0 NC A:HEM812 2.1 11.0 1.0 NA A:HEM812 2.1 11.3 1.0 NB A:HEM812 2.1 11.6 1.0 CD2 A:HIS502 3.1 10.5 1.0 C4C A:HEM812 3.1 10.4 1.0 C1C A:HEM812 3.1 10.7 1.0 C1A A:HEM812 3.1 10.7 1.0 C1D A:HEM812 3.1 10.5 1.0 CE1 A:HIS502 3.1 9.5 1.0 C4B A:HEM812 3.1 11.7 1.0 C4D A:HEM812 3.1 10.4 1.0 C4A A:HEM812 3.1 12.2 1.0 C1B A:HEM812 3.1 12.2 1.0 HD2 A:HIS502 3.2 12.6 1.0 O A:HOH1010 3.3 37.5 1.0 HE1 A:HIS502 3.3 11.4 1.0 CHC A:HEM812 3.4 11.4 1.0 CHA A:HEM812 3.4 10.4 1.0 CHD A:HEM812 3.5 10.9 1.0 CHB A:HEM812 3.5 12.9 1.0 HD21 A:LEU583 3.6 13.9 1.0 HG2 A:ARG499 4.0 11.7 1.0 CG A:HIS502 4.2 9.7 1.0 ND1 A:HIS502 4.2 9.4 1.0 C2C A:HEM812 4.3 11.4 1.0 C3C A:HEM812 4.3 10.9 1.0 HD11 A:LEU583 4.3 13.6 1.0 C2A A:HEM812 4.3 11.1 1.0 C3A A:HEM812 4.3 12.1 1.0 C3D A:HEM812 4.4 10.6 1.0 C2D A:HEM812 4.4 10.5 1.0 C3B A:HEM812 4.4 12.9 1.0 C2B A:HEM812 4.4 12.8 1.0 HHA A:HEM812 4.4 12.5 1.0 HHC A:HEM812 4.4 13.7 1.0 O A:HOH901 4.4 44.4 1.0 HHD A:HEM812 4.4 13.1 1.0 HHB A:HEM812 4.5 15.6 1.0 HG3 A:GLN257 4.5 13.8 1.0 HE21 A:GLN257 4.5 17.2 1.0 CD2 A:LEU583 4.5 11.6 1.0 HA A:ARG499 4.7 11.4 1.0 HB3 A:ARG499 4.8 11.8 1.0 HE2 A:HIS261 4.9 13.2 1.0 HD22 A:LEU583 4.9 13.9 1.0 CG A:ARG499 4.9 9.7 1.0

I.Grishkovskaya, M.Paumann-Page, R.Tscheliessnig, J.Stampler, S.Hofbauer, M.Soudi, B.Sevcnikar, C.Oostenbrink, P.G.Furtmuller, K.Djinovic-Carugo, W.M.Nauseef, C.Obinger. Structure of Human Promyeloperoxidase (Prompo) and the Role of the Propeptide in Processing and Maturation. J. Biol. Chem. V. 292 8244 2017.
ISSN: ESSN 1083-351X
PubMed: 28348079
DOI: 10.1074/JBC.M117.775031