Iron in PDB 4nfg: K13R Mutant of Horse Cytochrome C and Yeast Cytochrome C Peroxidase Complex

All present enzymatic activity of K13R Mutant of Horse Cytochrome C and Yeast Cytochrome C Peroxidase Complex:
1.11.1.5;

The structure of K13R Mutant of Horse Cytochrome C and Yeast Cytochrome C Peroxidase Complex, PDB code: 4nfg was solved by E.M.Meulenbroek, Q.Bashir, M.Ubbink, N.S.Pannu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	67.24 / 2.11
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	44.890, 87.700, 104.740, 90.00, 90.00, 90.00
R / Rfree (%)	17.4 / 23.6

The binding sites of Iron atom in the K13R Mutant of Horse Cytochrome C and Yeast Cytochrome C Peroxidase Complex (pdb code 4nfg). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the K13R Mutant of Horse Cytochrome C and Yeast Cytochrome C Peroxidase Complex, PDB code: 4nfg:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the K13R Mutant of Horse Cytochrome C and Yeast Cytochrome C Peroxidase Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of K13R Mutant of Horse Cytochrome C and Yeast Cytochrome C Peroxidase Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:10.2 occ:1.00 FE A:HEM301 0.0 10.2 1.0 ND A:HEM301 1.9 9.0 1.0 NA A:HEM301 2.0 9.5 1.0 NE2 A:HIS175 2.0 8.6 1.0 NC A:HEM301 2.1 8.9 1.0 NB A:HEM301 2.1 9.3 1.0 UNK A:UNX302 2.4 2.1 1.0 CE1 A:HIS175 2.9 8.5 1.0 C1D A:HEM301 2.9 8.7 1.0 C4D A:HEM301 3.0 9.7 1.0 C1A A:HEM301 3.0 9.4 1.0 C4A A:HEM301 3.0 9.8 1.0 C4B A:HEM301 3.0 9.3 1.0 C4C A:HEM301 3.0 8.7 1.0 CD2 A:HIS175 3.0 8.2 1.0 C1C A:HEM301 3.1 9.2 1.0 C1B A:HEM301 3.1 9.4 1.0 CHD A:HEM301 3.4 8.6 1.0 CHA A:HEM301 3.4 9.3 1.0 CHB A:HEM301 3.4 9.4 1.0 CHC A:HEM301 3.4 9.4 1.0 ND1 A:HIS175 4.0 8.4 1.0 CG A:HIS175 4.1 8.4 1.0 C2A A:HEM301 4.2 9.2 1.0 C3A A:HEM301 4.2 9.1 1.0 NE1 A:TRP51 4.2 8.3 1.0 C2D A:HEM301 4.2 8.9 1.0 C2C A:HEM301 4.2 9.2 1.0 C3C A:HEM301 4.2 9.1 1.0 C3D A:HEM301 4.3 9.3 1.0 C3B A:HEM301 4.3 9.2 1.0 C2B A:HEM301 4.3 9.0 1.0 O A:HOH458 4.4 19.0 1.0 CD1 A:TRP51 4.7 8.4 1.0 O A:HOH572 4.8 18.8 1.0 CH2 A:TRP191 5.0 8.7 1.0

Iron binding site 2 out of 2 in the K13R Mutant of Horse Cytochrome C and Yeast Cytochrome C Peroxidase Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of K13R Mutant of Horse Cytochrome C and Yeast Cytochrome C Peroxidase Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:15.8 occ:1.00 FE B:HEC201 0.0 15.8 1.0 ND B:HEC201 2.1 14.2 1.0 NE2 B:HIS18 2.1 13.2 1.0 NB B:HEC201 2.1 14.0 1.0 NA B:HEC201 2.1 14.5 1.0 NC B:HEC201 2.1 13.7 1.0 SD B:MET80 2.3 14.8 1.0 CD2 B:HIS18 3.0 14.2 1.0 C4D B:HEC201 3.1 15.2 1.0 C1B B:HEC201 3.1 14.2 1.0 C4A B:HEC201 3.1 14.1 1.0 C1C B:HEC201 3.1 13.0 1.0 CE1 B:HIS18 3.1 13.5 1.0 C1D B:HEC201 3.1 15.1 1.0 C1A B:HEC201 3.1 14.1 1.0 C4C B:HEC201 3.1 13.2 1.0 C4B B:HEC201 3.1 13.7 1.0 CE B:MET80 3.3 14.9 1.0 CG B:MET80 3.4 14.7 1.0 CHC B:HEC201 3.4 13.5 1.0 CHB B:HEC201 3.4 13.9 1.0 CHA B:HEC201 3.4 14.4 1.0 CHD B:HEC201 3.5 13.6 1.0 CB B:MET80 4.2 15.1 1.0 CG B:HIS18 4.2 13.7 1.0 ND1 B:HIS18 4.2 13.9 1.0 C3D B:HEC201 4.4 14.7 1.0 C3B B:HEC201 4.4 13.8 1.0 C2A B:HEC201 4.4 14.2 1.0 C3A B:HEC201 4.4 14.2 1.0 C2B B:HEC201 4.4 14.5 1.0 C2D B:HEC201 4.4 14.4 1.0 C3C B:HEC201 4.4 12.9 1.0 C2C B:HEC201 4.4 12.9 1.0 OH B:TYR67 4.8 18.2 1.0

Q.Bashir, E.M.Meulenbroek, N.S.Pannu, M.Ubbink. Engineering Specificity in A Dynamic Protein Complex with A Single Conserved Mutation. Febs J. V. 281 4892 2014.
ISSN: ISSN 1742-464X
PubMed: 25180929
DOI: 10.1111/FEBS.13028