Iron in PDB 4mu8: Crystal Structure of An Oxidized Form of Yeast Iso-1-Cytochrome C at pH 8.8

The structure of Crystal Structure of An Oxidized Form of Yeast Iso-1-Cytochrome C at pH 8.8, PDB code: 4mu8 was solved by L.J.Mcclelland, T.-C.Mou, M.E.Jeakins-Cooley, S.R.Sprang, B.E.Bowler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 1.45
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	93.621, 93.621, 155.014, 90.00, 90.00, 120.00
R / Rfree (%)	14.5 / 15.4

The binding sites of Iron atom in the Crystal Structure of An Oxidized Form of Yeast Iso-1-Cytochrome C at pH 8.8 (pdb code 4mu8). 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 An Oxidized Form of Yeast Iso-1-Cytochrome C at pH 8.8, PDB code: 4mu8:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of An Oxidized Form of Yeast Iso-1-Cytochrome C at pH 8.8


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 An Oxidized Form of Yeast Iso-1-Cytochrome C at pH 8.8 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:9.6 occ:1.00 FE A:HEM201 0.0 9.6 1.0 O A:HOH303 2.0 12.5 1.0 NE2 A:HIS18 2.0 9.1 1.0 NA A:HEM201 2.1 9.1 1.0 ND A:HEM201 2.1 9.8 1.0 NC A:HEM201 2.1 8.9 1.0 NB A:HEM201 2.2 11.2 1.0 CE1 A:HIS18 3.0 9.8 1.0 C1A A:HEM201 3.0 9.5 1.0 C1D A:HEM201 3.0 8.7 1.0 C4C A:HEM201 3.0 9.0 1.0 C4A A:HEM201 3.1 9.5 1.0 C4D A:HEM201 3.1 9.1 1.0 CD2 A:HIS18 3.1 9.4 1.0 C1C A:HEM201 3.1 9.1 1.0 C4B A:HEM201 3.1 10.3 1.0 C1B A:HEM201 3.1 9.9 1.0 HE1 A:HIS18 3.1 11.7 1.0 HD2 A:HIS18 3.3 11.3 1.0 CHD A:HEM201 3.4 9.1 1.0 CHA A:HEM201 3.4 9.7 1.0 CHB A:HEM201 3.5 10.1 1.0 CHC A:HEM201 3.5 10.4 1.0 HH A:TYR67 3.7 15.8 1.0 O A:HOH301 4.0 10.6 0.2 O A:HOH301 4.1 11.5 0.8 ND1 A:HIS18 4.1 9.5 1.0 CG A:HIS18 4.2 10.0 1.0 C2A A:HEM201 4.2 10.8 1.0 C3A A:HEM201 4.2 9.9 1.0 C3C A:HEM201 4.2 9.1 1.0 C2D A:HEM201 4.2 8.4 1.0 C3D A:HEM201 4.3 8.9 1.0 C2C A:HEM201 4.3 10.0 1.0 C2B A:HEM201 4.3 9.8 1.0 C3B A:HEM201 4.3 9.9 1.0 HE2 A:TYR67 4.4 15.4 1.0 OH A:TYR67 4.4 13.2 1.0 HA3 A:GLY29 4.8 12.6 1.0 HD11 A:LEU32 4.8 15.4 1.0 HD2 A:PRO30 4.8 11.4 1.0 HB2 A:CYS17 4.8 12.2 1.0 HD21 A:LEU32 4.8 15.0 1.0 HD1 A:HIS18 4.9 11.4 1.0 HD1 A:PHE82 5.0 18.1 1.0

Iron binding site 2 out of 2 in the Crystal Structure of An Oxidized Form of Yeast Iso-1-Cytochrome C at pH 8.8


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 An Oxidized Form of Yeast Iso-1-Cytochrome C at pH 8.8 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe202 b:10.1 occ:1.00 FE B:HEM202 0.0 10.1 1.0 O B:HOH305 2.0 12.6 1.0 NE2 B:HIS18 2.0 10.1 1.0 NA B:HEM202 2.0 8.8 1.0 ND B:HEM202 2.1 10.2 1.0 NC B:HEM202 2.1 8.7 1.0 NB B:HEM202 2.2 10.5 1.0 CE1 B:HIS18 3.0 9.1 1.0 C1A B:HEM202 3.0 10.4 1.0 CD2 B:HIS18 3.0 10.0 1.0 C4D B:HEM202 3.1 9.2 1.0 C4C B:HEM202 3.1 9.1 1.0 C1D B:HEM202 3.1 8.7 1.0 C4A B:HEM202 3.1 9.3 1.0 C1C B:HEM202 3.1 10.1 1.0 C4B B:HEM202 3.1 9.6 1.0 C1B B:HEM202 3.1 9.7 1.0 HE1 B:HIS18 3.2 10.9 1.0 HD2 B:HIS18 3.3 12.0 1.0 CHD B:HEM202 3.4 9.7 1.0 CHA B:HEM202 3.4 11.1 1.0 CHB B:HEM202 3.5 10.9 1.0 CHC B:HEM202 3.5 10.1 1.0 HH B:TYR67 3.7 14.8 1.0 O B:HOH303 4.0 12.1 0.4 O B:HOH303 4.1 10.1 0.6 ND1 B:HIS18 4.1 9.9 1.0 CG B:HIS18 4.2 9.5 1.0 C3A B:HEM202 4.2 9.7 1.0 C2A B:HEM202 4.2 11.7 1.0 C3C B:HEM202 4.2 9.8 1.0 C2D B:HEM202 4.3 8.8 1.0 C2C B:HEM202 4.3 9.8 1.0 C3D B:HEM202 4.3 10.0 1.0 C2B B:HEM202 4.3 9.8 1.0 C3B B:HEM202 4.3 10.1 1.0 HE2 B:TYR67 4.4 13.6 1.0 OH B:TYR67 4.4 12.4 1.0 HA3 B:GLY29 4.7 13.9 1.0 HD2 B:PRO30 4.8 13.8 1.0 HD11 B:LEU32 4.8 14.9 1.0 HB2 B:CYS17 4.8 13.2 1.0 HD1 B:HIS18 4.9 11.9 1.0 HD1 B:PHE82 4.9 18.9 1.0 HD21 B:LEU32 4.9 16.4 1.0

L.J.Mcclelland, T.C.Mou, M.E.Jeakins-Cooley, S.R.Sprang, B.E.Bowler. Structure of A Mitochondrial Cytochrome C Conformer Competent For Peroxidase Activity. Proc.Natl.Acad.Sci.Usa V. 111 6648 2014.
ISSN: ISSN 0027-8424
PubMed: 24760830
DOI: 10.1073/PNAS.1323828111