Iron in PDB 1d7w: Crystal Structure of Human Myeloperoxidase Isoform C Complexed with Cyanide and Bromide at pH 4.0

All present enzymatic activity of Crystal Structure of Human Myeloperoxidase Isoform C Complexed with Cyanide and Bromide at pH 4.0:
1.11.1.7;

The structure of Crystal Structure of Human Myeloperoxidase Isoform C Complexed with Cyanide and Bromide at pH 4.0, PDB code: 1d7w was solved by T.J.Fiedler, R.E.Fenna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	111.338, 63.324, 92.263, 90.00, 97.41, 90.00
R / Rfree (%)	21.5 / 27

The structure of Crystal Structure of Human Myeloperoxidase Isoform C Complexed with Cyanide and Bromide at pH 4.0 also contains other interesting chemical elements:

Bromine	(Br)	8 atoms
Calcium	(Ca)	2 atoms

The binding sites of Iron atom in the Crystal Structure of Human Myeloperoxidase Isoform C Complexed with Cyanide and Bromide at pH 4.0 (pdb code 1d7w). 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 Human Myeloperoxidase Isoform C Complexed with Cyanide and Bromide at pH 4.0, PDB code: 1d7w:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Human Myeloperoxidase Isoform C Complexed with Cyanide and Bromide at pH 4.0


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 Myeloperoxidase Isoform C Complexed with Cyanide and Bromide at pH 4.0 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe605 b:10.7 occ:1.00 FE A:HEM605 0.0 10.7 1.0 NB A:HEM605 2.0 4.6 1.0 NA A:HEM605 2.0 5.6 1.0 NC A:HEM605 2.0 5.3 1.0 ND A:HEM605 2.0 5.5 1.0 C A:CYN1844 2.1 6.8 1.0 NE2 C:HIS336 2.2 4.6 1.0 N A:CYN1844 2.8 6.6 1.0 C4B A:HEM605 3.0 6.2 1.0 C1B A:HEM605 3.0 5.8 1.0 C4A A:HEM605 3.0 5.7 1.0 C1D A:HEM605 3.0 5.3 1.0 C4C A:HEM605 3.0 5.8 1.0 C1A A:HEM605 3.0 6.5 1.0 C1C A:HEM605 3.0 2.3 1.0 C4D A:HEM605 3.0 3.6 1.0 CD2 C:HIS336 3.1 3.3 1.0 CE1 C:HIS336 3.2 3.4 1.0 CHB A:HEM605 3.4 4.3 1.0 CHD A:HEM605 3.4 5.0 1.0 CHC A:HEM605 3.4 2.3 1.0 CHA A:HEM605 3.4 5.0 1.0 CG C:HIS336 4.2 5.4 1.0 C3A A:HEM605 4.3 6.0 1.0 C2D A:HEM605 4.3 5.6 1.0 C2A A:HEM605 4.3 4.0 1.0 C3C A:HEM605 4.3 4.7 1.0 C2C A:HEM605 4.3 2.0 1.0 C3B A:HEM605 4.3 5.0 1.0 C3D A:HEM605 4.3 5.0 1.0 C2B A:HEM605 4.3 6.0 1.0 ND1 C:HIS336 4.3 5.7 1.0 CD2 C:LEU417 4.8 7.8 1.0 O C:HOH845A 4.8 6.0 1.0 NE2 A:GLN91 4.9 5.6 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Human Myeloperoxidase Isoform C Complexed with Cyanide and Bromide at pH 4.0


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 Human Myeloperoxidase Isoform C Complexed with Cyanide and Bromide at pH 4.0 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe605 b:10.2 occ:1.00 FE B:HEM605 0.0 10.2 1.0 NA B:HEM605 2.0 11.1 1.0 NC B:HEM605 2.0 5.7 1.0 NB B:HEM605 2.0 7.3 1.0 ND B:HEM605 2.0 7.4 1.0 C B:CYN2844 2.0 18.9 1.0 NE2 D:HIS336 2.2 10.5 1.0 N B:CYN2844 2.9 18.7 1.0 C4C B:HEM605 3.0 5.6 1.0 C1B B:HEM605 3.0 7.6 1.0 C4A B:HEM605 3.0 11.5 1.0 C1C B:HEM605 3.0 5.0 1.0 C1A B:HEM605 3.0 11.1 1.0 C1D B:HEM605 3.0 6.9 1.0 C4B B:HEM605 3.0 6.8 1.0 C4D B:HEM605 3.0 6.7 1.0 CD2 D:HIS336 3.2 8.8 1.0 CE1 D:HIS336 3.2 8.1 1.0 CHB B:HEM605 3.4 10.2 1.0 CHD B:HEM605 3.4 5.8 1.0 CHC B:HEM605 3.4 2.0 1.0 CHA B:HEM605 3.4 7.5 1.0 C2C B:HEM605 4.2 6.8 1.0 C3C B:HEM605 4.2 6.6 1.0 C3A B:HEM605 4.2 8.9 1.0 C2A B:HEM605 4.3 11.3 1.0 C2B B:HEM605 4.3 7.3 1.0 C3D B:HEM605 4.3 6.9 1.0 C3B B:HEM605 4.3 6.2 1.0 C2D B:HEM605 4.3 5.5 1.0 CG D:HIS336 4.3 10.2 1.0 ND1 D:HIS336 4.4 11.3 1.0 O B:HOH845B 4.6 16.1 1.0 CD2 D:LEU417 4.8 11.4 1.0 NE2 B:GLN91 4.9 3.8 1.0

M.Blair-Johnson, T.Fiedler, R.Fenna. Human Myeloperoxidase: Structure of A Cyanide Complex and Its Interaction with Bromide and Thiocyanate Substrates at 1.9 A Resolution. Biochemistry V. 40 13990 2001.
ISSN: ISSN 0006-2960
PubMed: 11705390
DOI: 10.1021/BI0111808