Iron in PDB 1sog: Cyrstal Structure of Cytochrome C Peroxidase Mutant: CCPK2M2

All present enzymatic activity of Cyrstal Structure of Cytochrome C Peroxidase Mutant: CCPK2M2:
1.11.1.5;

The structure of Cyrstal Structure of Cytochrome C Peroxidase Mutant: CCPK2M2, PDB code: 1sog was solved by T.P.Barrows, B.Bhaskar, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.85
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	106.790, 75.860, 51.380, 90.00, 90.00, 90.00
R / Rfree (%)	16.6 / 20.1

The structure of Cyrstal Structure of Cytochrome C Peroxidase Mutant: CCPK2M2 also contains other interesting chemical elements:

Potassium

(K)

1 atom

The binding sites of Iron atom in the Cyrstal Structure of Cytochrome C Peroxidase Mutant: CCPK2M2 (pdb code 1sog). 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 Cyrstal Structure of Cytochrome C Peroxidase Mutant: CCPK2M2, PDB code: 1sog:

Iron binding site 1 out of 1 in the Cyrstal Structure of Cytochrome C Peroxidase Mutant: CCPK2M2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cyrstal Structure of Cytochrome C Peroxidase Mutant: CCPK2M2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe296 b:10.6 occ:1.00 FE A:HEM296 0.0 10.6 1.0 NC A:HEM296 2.0 9.5 1.0 ND A:HEM296 2.0 9.8 1.0 NE2 A:HIS175 2.0 9.0 1.0 NB A:HEM296 2.0 9.5 1.0 NA A:HEM296 2.0 9.9 1.0 CD2 A:HIS175 3.0 9.3 1.0 CE1 A:HIS175 3.0 9.4 1.0 C1C A:HEM296 3.0 9.7 1.0 C4C A:HEM296 3.1 9.6 1.0 C1D A:HEM296 3.1 9.9 1.0 C4B A:HEM296 3.1 9.8 1.0 C4D A:HEM296 3.1 9.8 1.0 C1A A:HEM296 3.1 10.2 1.0 C4A A:HEM296 3.1 10.1 1.0 C1B A:HEM296 3.1 10.0 1.0 CHC A:HEM296 3.4 9.2 1.0 CHD A:HEM296 3.4 9.9 1.0 CHA A:HEM296 3.4 9.8 1.0 CHB A:HEM296 3.5 9.8 1.0 ND1 A:HIS175 4.1 9.2 1.0 NE1 A:TRP51 4.1 9.1 1.0 CG A:HIS175 4.1 9.0 1.0 NE A:ARG48 4.2 1.8 0.5 O A:HOH849 4.2 12.6 1.0 C3D A:HEM296 4.3 9.7 1.0 C2D A:HEM296 4.3 9.8 1.0 C2C A:HEM296 4.3 9.4 1.0 C3C A:HEM296 4.3 9.5 1.0 C3B A:HEM296 4.3 9.4 1.0 C2A A:HEM296 4.3 10.0 1.0 C2B A:HEM296 4.3 9.5 1.0 C3A A:HEM296 4.3 10.0 1.0 NH2 A:ARG48 4.7 1.0 0.5 CD1 A:TRP51 4.8 9.2 1.0 CZ A:ARG48 4.9 1.2 0.5 CH2 A:TRP191 5.0 9.6 1.0

T.P.Barrows, B.Bhaskar, T.L.Poulos. Electrostatic Control of the Tryptophan Radical in Cytochrome C Peroxidase. Biochemistry V. 43 8826 2004.
ISSN: ISSN 0006-2960
PubMed: 15236591
DOI: 10.1021/BI049531G