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Iron in PDB 8ogi: Structure of Native Human Eosinophil Peroxidase

Protein crystallography data

The structure of Structure of Native Human Eosinophil Peroxidase, PDB code: 8ogi was solved by V.Pfanzagl, C.Obinger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 22.57 / 1.55
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 53.123, 85.562, 139.395, 90, 90, 90
R / Rfree (%) 17.4 / 18.5

Other elements in 8ogi:

The structure of Structure of Native Human Eosinophil Peroxidase also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms
Calcium (Ca) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Native Human Eosinophil Peroxidase (pdb code 8ogi). 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 Structure of Native Human Eosinophil Peroxidase, PDB code: 8ogi:

Iron binding site 1 out of 1 in 8ogi

Go back to Iron Binding Sites List in 8ogi
Iron binding site 1 out of 1 in the Structure of Native Human Eosinophil Peroxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Native Human Eosinophil Peroxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe301

b:18.3
occ:1.00
FE A:HEB301 0.0 18.3 1.0
NA A:HEB301 2.0 17.4 1.0
ND A:HEB301 2.0 16.3 1.0
NC A:HEB301 2.1 16.9 1.0
NB A:HEB301 2.1 16.7 1.0
NE2 B:HIS474 2.2 17.9 1.0
O A:HOH438 2.9 25.8 1.0
C4D A:HEB301 3.1 16.6 1.0
CD2 B:HIS474 3.1 16.1 1.0
C4C A:HEB301 3.1 16.4 1.0
C1A A:HEB301 3.1 17.6 1.0
C4A A:HEB301 3.1 18.0 1.0
C1D A:HEB301 3.1 16.5 1.0
C4B A:HEB301 3.1 16.4 1.0
C1B A:HEB301 3.1 17.8 1.0
C1C A:HEB301 3.1 16.6 1.0
HD2 B:HIS474 3.2 14.8 0.0
CE1 B:HIS474 3.3 17.6 1.0
CHD A:HEB301 3.4 17.1 1.0
CHA A:HEB301 3.4 17.1 1.0
CHB A:HEB301 3.4 18.4 1.0
CHC A:HEB301 3.4 16.9 1.0
HE1 B:HIS474 3.5 16.2 0.0
HD21 B:LEU555 3.9 16.2 0.0
HE21 A:GLN229 4.1 18.0 0.0
HG2 B:ARG471 4.1 15.7 0.0
HG3 A:GLN229 4.2 15.7 0.0
CG B:HIS474 4.3 15.8 1.0
HD11 B:LEU555 4.3 16.2 0.0
C3D A:HEB301 4.3 15.7 1.0
C3C A:HEB301 4.3 16.6 1.0
C2A A:HEB301 4.3 17.3 1.0
C3A A:HEB301 4.3 17.5 1.0
C2D A:HEB301 4.3 15.8 1.0
C2C A:HEB301 4.3 16.8 1.0
C3B A:HEB301 4.3 17.1 1.0
C2B A:HEB301 4.3 17.6 1.0
ND1 B:HIS474 4.3 17.3 1.0
HHA A:HEB301 4.5 15.7 0.0
HHB A:HEB301 4.5 17.5 0.0
HHD A:HEB301 4.5 15.6 0.0
HHC A:HEB301 4.5 15.9 0.0
HA B:ARG471 4.5 12.9 0.0
O B:HOH925 4.6 35.4 1.0
NE2 A:GLN229 4.7 18.6 1.0
HB3 B:ARG471 4.8 13.9 0.0
CD2 B:LEU555 4.9 17.3 1.0

Reference:

V.Pfanzagl, C.Gruber-Grunwald, U.Leitgeb, P.G.Furtmuller, C.Obinger. Posttranslational Modification and Heme Cavity Architecture of Human Eosinophil Peroxidase-Insights From First Crystal Structure and Biochemical Characterization. J.Biol.Chem. V. 299 05402 2023.
ISSN: ESSN 1083-351X
PubMed: 38229400
DOI: 10.1016/J.JBC.2023.105402
Page generated: Thu Aug 7 18:58:50 2025

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