Iron in PDB 8dzl: Structure of the K39Q Mutant of Rat Somatic Cytochrome C at 1.36A

The structure of Structure of the K39Q Mutant of Rat Somatic Cytochrome C at 1.36A, PDB code: 8dzl was solved by B.F.P.Edwards, M.Huettemann, A.Vaishnav, J.Brunzelle, P.Morse, J.Wan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	58.10 / 1.36
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	33.578, 61.153, 186.065, 90, 90, 90
R / Rfree (%)	14.1 / 18

The binding sites of Iron atom in the Structure of the K39Q Mutant of Rat Somatic Cytochrome C at 1.36A (pdb code 8dzl). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Structure of the K39Q Mutant of Rat Somatic Cytochrome C at 1.36A, PDB code: 8dzl:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Structure of the K39Q Mutant of Rat Somatic Cytochrome C at 1.36A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of the K39Q Mutant of Rat Somatic Cytochrome C at 1.36A within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:14.9 occ:1.00 FE A:HEC201 0.0 14.9 1.0 NA A:HEC201 2.0 13.2 1.0 NE2 A:HIS18 2.0 13.0 1.0 NB A:HEC201 2.0 12.6 1.0 NC A:HEC201 2.0 13.7 1.0 ND A:HEC201 2.0 13.6 1.0 SD A:MET80 2.3 14.6 1.0 CE1 A:HIS18 3.0 14.4 1.0 C1A A:HEC201 3.0 11.2 1.0 C1D A:HEC201 3.0 13.6 1.0 CD2 A:HIS18 3.0 13.1 1.0 C1C A:HEC201 3.0 15.2 1.0 C4B A:HEC201 3.0 14.6 1.0 C1B A:HEC201 3.0 13.0 1.0 C4A A:HEC201 3.0 13.2 1.0 C4C A:HEC201 3.0 14.0 1.0 C4D A:HEC201 3.1 13.4 1.0 CG A:MET80 3.3 14.5 1.0 CHB A:HEC201 3.4 13.2 1.0 CHD A:HEC201 3.4 13.9 1.0 CE A:MET80 3.4 16.6 1.0 CHC A:HEC201 3.4 14.8 1.0 CHA A:HEC201 3.4 12.9 1.0 ND1 A:HIS18 4.1 13.0 1.0 CG A:HIS18 4.1 13.2 1.0 CB A:MET80 4.2 15.1 1.0 C2D A:HEC201 4.2 13.4 1.0 C3C A:HEC201 4.2 15.0 1.0 C3B A:HEC201 4.2 14.8 1.0 C2B A:HEC201 4.2 14.2 1.0 C2C A:HEC201 4.3 14.6 1.0 C2A A:HEC201 4.3 13.4 1.0 C3A A:HEC201 4.3 14.8 1.0 C3D A:HEC201 4.3 13.6 1.0 OH A:TYR67 4.8 18.1 1.0

Iron binding site 2 out of 4 in the Structure of the K39Q Mutant of Rat Somatic Cytochrome C at 1.36A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of the K39Q Mutant of Rat Somatic Cytochrome C at 1.36A within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:17.3 occ:1.00 FE B:HEC201 0.0 17.3 1.0 NE2 B:HIS18 1.9 14.9 1.0 NB B:HEC201 2.0 17.9 1.0 NA B:HEC201 2.0 14.8 1.0 ND B:HEC201 2.0 14.1 1.0 NC B:HEC201 2.0 16.7 1.0 SD B:MET80 2.3 16.8 1.0 CE1 B:HIS18 2.9 15.6 1.0 CD2 B:HIS18 3.0 15.7 1.0 C1B B:HEC201 3.0 15.2 1.0 C1D B:HEC201 3.0 15.4 1.0 C4B B:HEC201 3.0 17.8 1.0 C4A B:HEC201 3.0 14.7 1.0 C1A B:HEC201 3.0 14.2 1.0 C1C B:HEC201 3.0 16.9 1.0 C4D B:HEC201 3.0 14.0 1.0 C4C B:HEC201 3.1 15.5 1.0 CHB B:HEC201 3.3 15.5 1.0 CHD B:HEC201 3.4 16.0 1.0 CG B:MET80 3.4 17.2 1.0 CHA B:HEC201 3.4 14.8 1.0 CHC B:HEC201 3.4 17.8 1.0 CE B:MET80 3.5 20.9 1.0 ND1 B:HIS18 4.0 15.6 1.0 CG B:HIS18 4.1 14.6 1.0 C2D B:HEC201 4.2 15.1 1.0 C2B B:HEC201 4.2 16.2 1.0 C3B B:HEC201 4.2 16.9 1.0 C3C B:HEC201 4.3 17.1 1.0 C3D B:HEC201 4.3 14.1 1.0 C3A B:HEC201 4.3 15.8 1.0 C2A B:HEC201 4.3 14.0 1.0 CB B:MET80 4.3 16.8 1.0 C2C B:HEC201 4.3 18.7 1.0 OH B:TYR67 4.8 20.2 1.0

Iron binding site 3 out of 4 in the Structure of the K39Q Mutant of Rat Somatic Cytochrome C at 1.36A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of the K39Q Mutant of Rat Somatic Cytochrome C at 1.36A within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:14.2 occ:1.00 FE C:HEC201 0.0 14.2 1.0 NB C:HEC201 2.0 11.8 1.0 NA C:HEC201 2.0 11.2 1.0 NC C:HEC201 2.0 12.1 1.0 NE2 C:HIS18 2.0 12.5 1.0 ND C:HEC201 2.0 12.7 1.0 SD C:MET80 2.3 13.3 1.0 CE1 C:HIS18 3.0 12.2 1.0 C4A C:HEC201 3.0 11.9 1.0 C1B C:HEC201 3.0 12.3 1.0 C1C C:HEC201 3.0 13.4 1.0 C4B C:HEC201 3.0 11.9 1.0 C1D C:HEC201 3.0 12.4 1.0 CD2 C:HIS18 3.0 13.4 1.0 C1A C:HEC201 3.0 11.6 1.0 C4C C:HEC201 3.0 12.6 1.0 C4D C:HEC201 3.1 11.7 1.0 CE C:MET80 3.4 16.1 1.0 CHD C:HEC201 3.4 12.6 1.0 CHB C:HEC201 3.4 12.0 1.0 CG C:MET80 3.4 13.6 1.0 CHC C:HEC201 3.4 13.3 1.0 CHA C:HEC201 3.5 12.0 1.0 ND1 C:HIS18 4.1 13.8 1.0 CG C:HIS18 4.1 13.3 1.0 CB C:MET80 4.2 13.4 1.0 C2B C:HEC201 4.2 13.3 1.0 C3B C:HEC201 4.2 12.9 1.0 C2C C:HEC201 4.2 13.0 1.0 C3C C:HEC201 4.3 13.1 1.0 C2D C:HEC201 4.3 13.2 1.0 C3A C:HEC201 4.3 12.1 1.0 C2A C:HEC201 4.3 12.4 1.0 C3D C:HEC201 4.3 12.5 1.0 OH C:TYR67 4.8 16.8 1.0

Iron binding site 4 out of 4 in the Structure of the K39Q Mutant of Rat Somatic Cytochrome C at 1.36A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of the K39Q Mutant of Rat Somatic Cytochrome C at 1.36A within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe201 b:13.1 occ:1.00 FE D:HEC201 0.0 13.1 1.0 NE2 D:HIS18 2.0 11.9 1.0 NA D:HEC201 2.0 11.1 1.0 NC D:HEC201 2.0 12.2 1.0 NB D:HEC201 2.0 12.0 1.0 ND D:HEC201 2.0 11.3 1.0 SD D:MET80 2.3 13.4 1.0 CE1 D:HIS18 2.9 12.2 1.0 CD2 D:HIS18 3.0 12.6 1.0 C4B D:HEC201 3.0 12.4 1.0 C1C D:HEC201 3.0 12.9 1.0 C4A D:HEC201 3.0 13.0 1.0 C1A D:HEC201 3.0 11.3 1.0 C1D D:HEC201 3.0 12.0 1.0 C1B D:HEC201 3.0 12.5 1.0 C4D D:HEC201 3.0 11.7 1.0 C4C D:HEC201 3.1 13.2 1.0 CHB D:HEC201 3.4 12.7 1.0 CHD D:HEC201 3.4 13.0 1.0 CG D:MET80 3.4 14.1 1.0 CHA D:HEC201 3.4 11.9 1.0 CE D:MET80 3.4 15.1 1.0 CHC D:HEC201 3.4 12.9 1.0 ND1 D:HIS18 4.1 13.7 1.0 CG D:HIS18 4.1 13.4 1.0 C2D D:HEC201 4.2 13.2 1.0 CB D:MET80 4.2 13.8 1.0 C3B D:HEC201 4.2 13.1 1.0 C3A D:HEC201 4.2 11.5 1.0 C2B D:HEC201 4.3 13.2 1.0 C2A D:HEC201 4.3 12.0 1.0 C3C D:HEC201 4.3 12.7 1.0 C2C D:HEC201 4.3 12.8 1.0 C3D D:HEC201 4.3 12.4 1.0 OH D:TYR67 4.8 16.9 1.0

P.R.Morse, H.Kalpage, J.Wan, A.Vaishnav, D.D.Chowdhury, J.S.Brunzelle, B.F.P.Edwards, M.Huettemann. Lysine 39 Acetylation of Cytochrome C in Ischemic Skeletal Muscle Stimulates Respiration While Attenuating Cell Death Nat Commun 2023.
ISSN: ESSN 2041-1723
DOI: 10.1038/S41467-023-39820-8