Iron in PDB 3ew0: The Novel 2FE-2S Outer Mitochondrial Protein Mitoneet Displays Conformational Flexibility in Its N-Terminal Cytoplasmic Tethering Domain

The structure of The Novel 2FE-2S Outer Mitochondrial Protein Mitoneet Displays Conformational Flexibility in Its N-Terminal Cytoplasmic Tethering Domain, PDB code: 3ew0 was solved by A.R.Conlan, M.L.Paddock, S.Wiley, H.L.Axelrod, A.E.Cohen, E.C.Abresch, M.Roy, R.Nechushtai, P.A.Jennings, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.55 / 1.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	50.737, 48.476, 59.245, 90.00, 90.00, 90.00
R / Rfree (%)	19.8 / 24.1

The binding sites of Iron atom in the The Novel 2FE-2S Outer Mitochondrial Protein Mitoneet Displays Conformational Flexibility in Its N-Terminal Cytoplasmic Tethering Domain (pdb code 3ew0). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the The Novel 2FE-2S Outer Mitochondrial Protein Mitoneet Displays Conformational Flexibility in Its N-Terminal Cytoplasmic Tethering Domain, PDB code: 3ew0:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the The Novel 2FE-2S Outer Mitochondrial Protein Mitoneet Displays Conformational Flexibility in Its N-Terminal Cytoplasmic Tethering Domain


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Novel 2FE-2S Outer Mitochondrial Protein Mitoneet Displays Conformational Flexibility in Its N-Terminal Cytoplasmic Tethering Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:6.9 occ:1.00 FE1 A:FES500 0.0 6.9 1.0 S1 A:FES500 2.2 7.8 1.0 S2 A:FES500 2.2 7.3 1.0 SG A:CYS74 2.2 4.1 1.0 SG A:CYS72 2.4 3.5 1.0 FE2 A:FES500 2.7 8.1 1.0 CB A:CYS74 3.3 3.7 1.0 CB A:CYS72 3.4 2.0 1.0 N A:CYS74 3.6 3.1 1.0 CA A:CYS72 3.8 3.0 1.0 CA A:CYS74 3.9 3.4 1.0 N A:ARG73 3.9 3.3 1.0 CB A:HIS87 4.0 5.8 1.0 ND1 A:HIS87 4.2 6.7 1.0 N A:HIS87 4.2 5.6 1.0 C A:CYS72 4.3 2.7 1.0 N A:TRP75 4.4 3.5 1.0 N A:SER77 4.4 4.8 1.0 C A:CYS74 4.4 3.8 1.0 CB A:SER77 4.5 5.1 1.0 CA A:HIS87 4.5 5.6 1.0 CG A:HIS87 4.6 6.1 1.0 C A:ARG73 4.6 3.3 1.0 N A:ARG76 4.7 4.4 1.0 SG A:CYS83 4.7 4.8 1.0 CA A:CYS83 4.8 5.1 1.0 CA A:ARG73 4.9 3.0 1.0 CA A:SER77 4.9 5.2 1.0 CB A:CYS83 4.9 4.9 1.0

Iron binding site 2 out of 4 in the The Novel 2FE-2S Outer Mitochondrial Protein Mitoneet Displays Conformational Flexibility in Its N-Terminal Cytoplasmic Tethering Domain


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The Novel 2FE-2S Outer Mitochondrial Protein Mitoneet Displays Conformational Flexibility in Its N-Terminal Cytoplasmic Tethering Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:8.1 occ:1.00 FE2 A:FES500 0.0 8.1 1.0 ND1 A:HIS87 2.0 6.7 1.0 S1 A:FES500 2.2 7.8 1.0 S2 A:FES500 2.2 7.3 1.0 SG A:CYS83 2.3 4.8 1.0 FE1 A:FES500 2.7 6.9 1.0 CE1 A:HIS87 2.9 6.4 1.0 CG A:HIS87 3.1 6.1 1.0 CB A:CYS83 3.4 4.9 1.0 CB A:HIS87 3.6 5.8 1.0 CA A:CYS83 3.9 5.1 1.0 N A:HIS87 3.9 5.6 1.0 N A:GLY85 4.0 6.0 1.0 NE2 A:HIS87 4.1 6.6 1.0 CD2 A:HIS87 4.2 6.6 1.0 CD A:PRO100 4.3 5.0 1.0 N A:ASP84 4.3 5.8 1.0 CA A:GLY85 4.3 5.8 1.0 CB A:PRO100 4.4 5.0 1.0 CA A:HIS87 4.4 5.6 1.0 SG A:CYS74 4.4 4.1 1.0 N A:ALA86 4.5 5.1 1.0 CG A:PRO100 4.5 4.9 1.0 C A:CYS83 4.5 5.6 1.0 C A:GLY85 4.6 5.5 1.0 SG A:CYS72 4.6 3.5 1.0 CA A:CYS72 4.7 3.0 1.0 CB A:CYS72 4.8 2.0 1.0 N A:PRO100 4.8 5.2 1.0

Iron binding site 3 out of 4 in the The Novel 2FE-2S Outer Mitochondrial Protein Mitoneet Displays Conformational Flexibility in Its N-Terminal Cytoplasmic Tethering Domain


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of The Novel 2FE-2S Outer Mitochondrial Protein Mitoneet Displays Conformational Flexibility in Its N-Terminal Cytoplasmic Tethering Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:6.4 occ:1.00 FE1 B:FES500 0.0 6.4 1.0 S2 B:FES500 2.2 6.2 1.0 S1 B:FES500 2.2 8.7 1.0 SG B:CYS74 2.3 3.7 1.0 SG B:CYS72 2.3 3.8 1.0 FE2 B:FES500 2.7 7.4 1.0 CB B:CYS74 3.3 4.2 1.0 CB B:CYS72 3.4 2.5 1.0 N B:CYS74 3.5 3.1 1.0 CA B:CYS72 3.8 3.2 1.0 CA B:CYS74 3.9 3.5 1.0 N B:ARG73 4.0 2.7 1.0 CB B:HIS87 4.0 4.6 1.0 ND1 B:HIS87 4.2 5.4 1.0 C B:CYS72 4.3 2.9 1.0 N B:HIS87 4.3 4.7 1.0 N B:TRP75 4.3 3.7 1.0 N B:SER77 4.4 4.5 1.0 C B:CYS74 4.4 3.7 1.0 CB B:SER77 4.5 4.8 1.0 N B:ARG76 4.5 4.7 1.0 CG B:HIS87 4.6 5.5 1.0 CA B:HIS87 4.6 4.4 1.0 C B:ARG73 4.6 3.0 1.0 SG B:CYS83 4.7 6.1 1.0 CA B:CYS83 4.9 5.5 1.0 CA B:ARG73 4.9 2.6 1.0 CA B:SER77 4.9 5.1 1.0 CB B:CYS83 5.0 5.3 1.0

Iron binding site 4 out of 4 in the The Novel 2FE-2S Outer Mitochondrial Protein Mitoneet Displays Conformational Flexibility in Its N-Terminal Cytoplasmic Tethering Domain


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of The Novel 2FE-2S Outer Mitochondrial Protein Mitoneet Displays Conformational Flexibility in Its N-Terminal Cytoplasmic Tethering Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:7.4 occ:1.00 FE2 B:FES500 0.0 7.4 1.0 ND1 B:HIS87 2.0 5.4 1.0 S1 B:FES500 2.2 8.7 1.0 S2 B:FES500 2.3 6.2 1.0 SG B:CYS83 2.3 6.1 1.0 FE1 B:FES500 2.7 6.4 1.0 CE1 B:HIS87 2.9 5.8 1.0 CG B:HIS87 3.1 5.5 1.0 CB B:CYS83 3.4 5.3 1.0 CB B:HIS87 3.6 4.6 1.0 CA B:CYS83 3.9 5.5 1.0 N B:HIS87 4.0 4.7 1.0 NE2 B:HIS87 4.1 6.0 1.0 N B:GLY85 4.1 4.7 1.0 CD2 B:HIS87 4.2 5.8 1.0 CD B:PRO100 4.3 3.7 1.0 CB B:PRO100 4.3 3.8 1.0 N B:ASP84 4.4 5.4 1.0 CA B:GLY85 4.4 4.7 1.0 SG B:CYS74 4.4 3.7 1.0 CA B:HIS87 4.5 4.4 1.0 N B:ALA86 4.5 4.4 1.0 CG B:PRO100 4.5 3.5 1.0 C B:CYS83 4.5 5.8 1.0 SG B:CYS72 4.6 3.8 1.0 C B:GLY85 4.6 4.8 1.0 CA B:CYS72 4.7 3.2 1.0 N B:PRO100 4.8 3.4 1.0 CB B:CYS72 4.8 2.5 1.0 CA B:PRO100 5.0 3.9 1.0

A.R.Conlan, M.L.Paddock, H.L.Axelrod, A.E.Cohen, E.C.Abresch, S.Wiley, M.Roy, R.Nechushtai, P.A.Jennings. The Novel 2FE-2S Outer Mitochondrial Protein Mitoneet Displays Conformational Flexibility in Its N-Terminal Cytoplasmic Tethering Domain. Acta Crystallogr.,Sect.F V. 65 654 2009.
ISSN: ESSN 1744-3091
PubMed: 19574633
DOI: 10.1107/S1744309109019605