Iron in PDB 12cl: Crystal Structure of Canine Myeloperoxidase Inhibited By Spin From Staphylococcus Delphini

All present enzymatic activity of Crystal Structure of Canine Myeloperoxidase Inhibited By Spin From Staphylococcus Delphini:
1.11.2.2;

The structure of Crystal Structure of Canine Myeloperoxidase Inhibited By Spin From Staphylococcus Delphini, PDB code: 12cl was solved by S.Fatehi, B.V.Geisbrecht, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.42 / 2.10
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	132.697, 145.377, 107.61, 90, 114.85, 90
R / Rfree (%)	16.7 / 19.9

The structure of Crystal Structure of Canine Myeloperoxidase Inhibited By Spin From Staphylococcus Delphini also contains other interesting chemical elements:

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

The binding sites of Iron atom in the Crystal Structure of Canine Myeloperoxidase Inhibited By Spin From Staphylococcus Delphini (pdb code 12cl). 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 Canine Myeloperoxidase Inhibited By Spin From Staphylococcus Delphini, PDB code: 12cl:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Canine Myeloperoxidase Inhibited By Spin From Staphylococcus Delphini


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 Canine Myeloperoxidase Inhibited By Spin From Staphylococcus Delphini within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe802 b:26.9 occ:1.00 FE A:HEM802 0.0 26.9 1.0 ND A:HEM802 2.1 21.0 1.0 NB A:HEM802 2.1 31.4 1.0 NA A:HEM802 2.1 29.0 1.0 NE2 A:HIS502 2.1 26.2 1.0 NC A:HEM802 2.1 27.6 1.0 C4D A:HEM802 3.1 24.7 1.0 CD2 A:HIS502 3.1 26.4 1.0 O A:HOH1118 3.1 35.3 1.0 C1A A:HEM802 3.1 29.2 1.0 C1C A:HEM802 3.1 27.5 1.0 C4B A:HEM802 3.1 30.4 1.0 C4C A:HEM802 3.1 26.6 1.0 C1B A:HEM802 3.1 30.7 1.0 C1D A:HEM802 3.1 26.1 1.0 C4A A:HEM802 3.1 26.9 1.0 CE1 A:HIS502 3.1 24.4 1.0 CHA A:HEM802 3.4 25.8 1.0 CHC A:HEM802 3.4 28.2 1.0 CHB A:HEM802 3.5 30.6 1.0 CHD A:HEM802 3.5 21.1 1.0 CG A:HIS502 4.2 25.6 1.0 ND1 A:HIS502 4.2 25.1 1.0 C2C A:HEM802 4.3 26.6 1.0 C3D A:HEM802 4.3 25.4 1.0 C3C A:HEM802 4.3 26.1 1.0 C2A A:HEM802 4.3 30.9 1.0 C3B A:HEM802 4.3 34.9 1.0 C2D A:HEM802 4.3 25.3 1.0 C3A A:HEM802 4.3 28.9 1.0 C2B A:HEM802 4.3 35.4 1.0 CD2 A:LEU583 4.5 27.7 1.0 NE2 A:GLN257 4.9 30.3 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Canine Myeloperoxidase Inhibited By Spin From Staphylococcus Delphini


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 Canine Myeloperoxidase Inhibited By Spin From Staphylococcus Delphini within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe807 b:29.6 occ:1.00 FE B:HEM807 0.0 29.6 1.0 ND B:HEM807 2.1 27.9 1.0 NA B:HEM807 2.1 31.2 1.0 NC B:HEM807 2.1 26.1 1.0 NB B:HEM807 2.1 31.9 1.0 NE2 B:HIS502 2.2 26.6 1.0 O B:HOH1056 2.8 34.6 1.0 C1A B:HEM807 3.1 30.3 1.0 C4D B:HEM807 3.1 27.2 1.0 C1D B:HEM807 3.1 26.7 1.0 C1C B:HEM807 3.1 29.7 1.0 C4A B:HEM807 3.1 33.4 1.0 CD2 B:HIS502 3.1 29.5 1.0 C4C B:HEM807 3.1 29.3 1.0 C4B B:HEM807 3.1 28.0 1.0 C1B B:HEM807 3.1 32.9 1.0 CE1 B:HIS502 3.2 25.7 1.0 CHA B:HEM807 3.4 26.9 1.0 CHD B:HEM807 3.4 26.0 1.0 CHC B:HEM807 3.5 29.8 1.0 CHB B:HEM807 3.5 32.2 1.0 C2C B:HEM807 4.3 29.4 1.0 C2A B:HEM807 4.3 31.8 1.0 CG B:HIS502 4.3 27.5 1.0 C3C B:HEM807 4.3 28.1 1.0 C3A B:HEM807 4.3 29.7 1.0 C2D B:HEM807 4.3 26.4 1.0 C3D B:HEM807 4.3 26.1 1.0 ND1 B:HIS502 4.3 30.4 1.0 C3B B:HEM807 4.3 33.7 1.0 C2B B:HEM807 4.3 35.4 1.0 CD2 B:LEU583 4.5 32.4 1.0

S.Fatehi, B.V.Geisbrecht. Staphylococcal Peroxidase Inhibitor: Structure/Function Studies on Host-Species Specificity To Be Published.