Iron in PDB 1zby: High-Resolution Crystal Structure of Native (Resting) Cytochrome C Peroxidase (Ccp)

All present enzymatic activity of High-Resolution Crystal Structure of Native (Resting) Cytochrome C Peroxidase (Ccp):
1.11.1.5;

The structure of High-Resolution Crystal Structure of Native (Resting) Cytochrome C Peroxidase (Ccp), PDB code: 1zby was solved by C.A.Bonagura, B.Bhaskar, H.Shimizu, H.Li, M.Sundaramoorthy, D.E.Mcree, D.B.Goodin, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	100.00 / 1.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	106.673, 75.513, 50.994, 90.00, 90.00, 90.00
R / Rfree (%)	11.3 / 14.9

The binding sites of Iron atom in the High-Resolution Crystal Structure of Native (Resting) Cytochrome C Peroxidase (Ccp) (pdb code 1zby). 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 High-Resolution Crystal Structure of Native (Resting) Cytochrome C Peroxidase (Ccp), PDB code: 1zby:

Iron binding site 1 out of 1 in the High-Resolution Crystal Structure of Native (Resting) Cytochrome C Peroxidase (Ccp)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of High-Resolution Crystal Structure of Native (Resting) Cytochrome C Peroxidase (Ccp) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe296 b:7.7 occ:1.00 FE A:HEM296 0.0 7.7 1.0 NC A:HEM296 2.0 8.4 1.0 ND A:HEM296 2.0 8.4 1.0 NB A:HEM296 2.1 8.6 1.0 NA A:HEM296 2.1 8.7 1.0 NE2 A:HIS175 2.1 8.5 1.0 O A:HOH1232 2.3 50.3 1.0 C4B A:HEM296 3.1 8.0 1.0 C4C A:HEM296 3.1 7.4 1.0 C1C A:HEM296 3.1 7.5 1.0 C1D A:HEM296 3.1 7.6 1.0 CE1 A:HIS175 3.1 9.2 1.0 C4D A:HEM296 3.1 8.8 1.0 C1A A:HEM296 3.1 8.3 1.0 C4A A:HEM296 3.1 8.9 1.0 C1B A:HEM296 3.1 9.2 1.0 CD2 A:HIS175 3.1 9.0 1.0 CHC A:HEM296 3.4 8.0 1.0 CHD A:HEM296 3.4 7.6 1.0 CHA A:HEM296 3.5 9.2 1.0 CHB A:HEM296 3.5 9.2 1.0 NE1 A:TRP51 4.1 11.5 1.0 NE A:ARG48 4.2 10.5 0.6 ND1 A:HIS175 4.2 8.8 1.0 O A:HOH643 4.3 24.2 0.5 O A:HOH640 4.3 18.0 1.0 CG A:HIS175 4.3 7.9 1.0 C3D A:HEM296 4.3 8.1 1.0 C2D A:HEM296 4.3 7.7 1.0 C3C A:HEM296 4.3 7.7 1.0 C3B A:HEM296 4.3 8.4 1.0 C2C A:HEM296 4.3 7.6 1.0 C2A A:HEM296 4.3 8.5 1.0 C3A A:HEM296 4.3 9.1 1.0 C2B A:HEM296 4.3 8.9 1.0 CD1 A:TRP51 4.6 10.8 1.0 NH2 A:ARG48 4.7 9.4 0.6 CG A:ARG48 4.9 9.9 0.6 CH2 A:TRP191 5.0 10.3 1.0 CD A:ARG48 5.0 11.1 0.6 CZ A:ARG48 5.0 11.3 0.6

C.A.Bonagura, B.Bhaskar, H.Shimizu, H.Li, M.Sundaramoorthy, D.E.Mcree, D.B.Goodin, T.L.Poulos. High-Resolution Crystal Structures and Spectroscopy of Native and Compound I Cytochrome C Peroxidase Biochemistry V. 42 5600 2003.
ISSN: ISSN 0006-2960
PubMed: 12741816
DOI: 10.1021/BI034058C