Iron in PDB 2jti: Solution Structure of the Yeast Iso-1-Cytochrome C (T12A) : Yeast Cytochrome C Peroxidase Complex

All present enzymatic activity of Solution Structure of the Yeast Iso-1-Cytochrome C (T12A) : Yeast Cytochrome C Peroxidase Complex:
1.11.1.5;

The binding sites of Iron atom in the Solution Structure of the Yeast Iso-1-Cytochrome C (T12A) : Yeast Cytochrome C Peroxidase Complex (pdb code 2jti). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Solution Structure of the Yeast Iso-1-Cytochrome C (T12A) : Yeast Cytochrome C Peroxidase Complex, PDB code: 2jti:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Solution Structure of the Yeast Iso-1-Cytochrome C (T12A) : 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 Solution Structure of the Yeast Iso-1-Cytochrome C (T12A) : Yeast Cytochrome C Peroxidase Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe295 b:17.3 occ:1.00 FE A:HEM295 0.0 17.3 1.0 NE2 A:HIS175 1.9 4.3 1.0 NA A:HEM295 2.0 18.0 1.0 NC A:HEM295 2.0 17.1 1.0 ND A:HEM295 2.1 19.8 1.0 NB A:HEM295 2.1 20.5 1.0 CE1 A:HIS175 2.8 7.7 1.0 HE1 A:HIS175 2.9 0.0 1.0 C1A A:HEM295 3.0 19.9 1.0 C4A A:HEM295 3.0 19.5 1.0 C4C A:HEM295 3.0 21.6 1.0 C1D A:HEM295 3.0 19.1 1.0 C1C A:HEM295 3.1 20.2 1.0 CD2 A:HIS175 3.1 6.5 1.0 C4D A:HEM295 3.1 17.6 1.0 C1B A:HEM295 3.1 19.1 1.0 C4B A:HEM295 3.2 17.0 1.0 CHB A:HEM295 3.4 17.4 1.0 CHD A:HEM295 3.4 15.1 1.0 HD2 A:HIS175 3.4 0.0 1.0 CHA A:HEM295 3.5 17.5 1.0 CHC A:HEM295 3.5 18.7 1.0 ND1 A:HIS175 4.0 2.2 1.0 CG A:HIS175 4.2 7.3 1.0 C2A A:HEM295 4.2 18.4 1.0 C3A A:HEM295 4.2 17.4 1.0 C3D A:HEM295 4.3 18.7 1.0 HG3 A:ARG48 4.3 0.0 1.0 C2C A:HEM295 4.3 19.6 1.0 C2D A:HEM295 4.3 19.7 1.0 C3C A:HEM295 4.3 19.6 1.0 C2B A:HEM295 4.4 18.4 1.0 C3B A:HEM295 4.4 18.1 1.0 HHD A:HEM295 4.5 0.0 1.0 HHB A:HEM295 4.5 0.0 1.0 HHA A:HEM295 4.5 0.0 1.0 HHC A:HEM295 4.5 0.0 1.0 HE A:ARG48 4.5 0.0 1.0 HE1 A:TRP51 4.6 0.0 1.0 HH2 A:TRP191 4.6 0.0 1.0 HD1 A:TRP51 4.7 0.0 1.0 HZ2 A:TRP191 4.8 0.0 1.0 HD1 A:HIS175 4.9 0.0 1.0

Iron binding site 2 out of 2 in the Solution Structure of the Yeast Iso-1-Cytochrome C (T12A) : 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 Solution Structure of the Yeast Iso-1-Cytochrome C (T12A) : Yeast Cytochrome C Peroxidase Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe104 b:26.0 occ:1.00 FE B:HEC104 0.0 26.0 1.0 NE2 B:HIS18 1.9 4.1 1.0 NB B:HEC104 2.0 28.1 1.0 NA B:HEC104 2.0 30.5 1.0 ND B:HEC104 2.0 30.8 1.0 NC B:HEC104 2.1 31.3 1.0 SD B:MET80 2.2 21.3 1.0 CE1 B:HIS18 2.8 9.7 1.0 C1B B:HEC104 3.0 29.4 1.0 HE1 B:HIS18 3.0 0.0 1.0 C4B B:HEC104 3.0 28.1 1.0 C4A B:HEC104 3.0 31.0 1.0 CD2 B:HIS18 3.0 3.0 1.0 C4D B:HEC104 3.1 31.4 1.0 C1D B:HEC104 3.1 30.6 1.0 C1C B:HEC104 3.1 31.1 1.0 C1A B:HEC104 3.1 30.4 1.0 C4C B:HEC104 3.1 30.9 1.0 CE B:MET80 3.3 16.6 1.0 HE1 B:MET80 3.3 0.0 1.0 CHB B:HEC104 3.3 31.9 1.0 HD2 B:HIS18 3.4 0.0 1.0 CHC B:HEC104 3.4 30.5 1.0 CHD B:HEC104 3.4 30.6 1.0 CHA B:HEC104 3.5 31.5 1.0 HB2 B:MET80 3.5 0.0 1.0 HE3 B:MET80 3.6 0.0 1.0 CG B:MET80 3.7 19.8 1.0 HB3 B:MET80 3.9 0.0 1.0 CB B:MET80 3.9 26.1 1.0 ND1 B:HIS18 4.0 8.6 1.0 HG2 B:MET80 4.1 0.0 1.0 CG B:HIS18 4.1 9.0 1.0 C2B B:HEC104 4.2 29.4 1.0 HE2 B:MET80 4.3 0.0 1.0 C3B B:HEC104 4.3 27.7 1.0 C3D B:HEC104 4.3 31.5 1.0 C2A B:HEC104 4.3 33.2 1.0 C3A B:HEC104 4.3 33.3 1.0 C2D B:HEC104 4.3 33.0 1.0 C2C B:HEC104 4.3 32.5 1.0 C3C B:HEC104 4.3 31.8 1.0 HHB B:HEC104 4.4 0.0 1.0 HHD B:HEC104 4.5 0.0 1.0 HHC B:HEC104 4.5 0.0 1.0 HG3 B:MET80 4.5 0.0 1.0 HHA B:HEC104 4.5 0.0 1.0 HE2 B:TYR67 4.6 0.0 1.0 HB2 B:CYS17 4.6 0.0 1.0 HD2 B:PRO30 4.6 0.0 1.0 HD1 B:HIS18 4.9 0.0 1.0 HD12 B:LEU32 5.0 0.0 1.0

A.N.Volkov, Q.Bashir, J.A.Worrall, G.M.Ullmann, M.Ubbink. Shifting the Equilibrium Between the Encounter State and the Specific Form of A Protein Complex By Interfacial Point Mutations. J.Am.Chem.Soc. V. 132 11487 2010.
ISSN: ISSN 0002-7863
PubMed: 20672804
DOI: 10.1021/JA100867C