Iron in PDB 9gs2: Structure of the Rieske Bound APO1 State of the Heptameric BCS1 Aaa- Atpase

All present enzymatic activity of Structure of the Rieske Bound APO1 State of the Heptameric BCS1 Aaa- Atpase:
7.1.1.8;

The binding sites of Iron atom in the Structure of the Rieske Bound APO1 State of the Heptameric BCS1 Aaa- Atpase (pdb code 9gs2). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of the Rieske Bound APO1 State of the Heptameric BCS1 Aaa- Atpase, PDB code: 9gs2:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of the Rieske Bound APO1 State of the Heptameric BCS1 Aaa- Atpase


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 Rieske Bound APO1 State of the Heptameric BCS1 Aaa- Atpase within 5.0Å range: probe atom residue distance (Å) B Occ H:Fe301 b:233.6 occ:1.00 FE1 H:FES301 0.0 233.6 1.0 ND1 H:HIS181 2.1 176.7 1.0 ND1 H:HIS161 2.2 176.1 1.0 S2 H:FES301 2.2 230.0 1.0 S1 H:FES301 2.2 227.8 1.0 FE2 H:FES301 2.7 229.6 1.0 CG H:HIS181 2.8 174.9 1.0 CG H:HIS161 3.0 174.2 1.0 CB H:HIS181 3.1 174.0 1.0 CE1 H:HIS181 3.1 175.9 1.0 CE1 H:HIS161 3.2 174.3 1.0 CB H:HIS161 3.2 174.4 1.0 SG H:CYS159 3.6 182.3 1.0 N H:HIS181 3.8 172.4 1.0 CD2 H:HIS181 3.9 173.5 1.0 CA H:HIS181 4.0 172.2 1.0 NE2 H:HIS181 4.0 174.0 1.0 CD2 H:HIS161 4.2 173.2 1.0 CD2 H:LEU162 4.3 174.1 1.0 NE2 H:HIS161 4.3 172.7 1.0 CG H:PRO195 4.3 155.7 1.0 OG H:SER183 4.4 152.8 1.0 C H:HIS181 4.5 172.0 1.0 N H:LEU162 4.5 172.9 1.0 CA H:HIS161 4.6 173.8 1.0 CB H:CYS180 4.6 179.4 1.0 C H:CYS180 4.7 176.9 1.0 O H:HIS181 4.8 172.6 1.0 CB H:CYS159 4.8 180.6 1.0 C H:HIS161 4.8 173.5 1.0 SG H:CYS178 4.9 164.7 1.0

Iron binding site 2 out of 2 in the Structure of the Rieske Bound APO1 State of the Heptameric BCS1 Aaa- Atpase


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 Rieske Bound APO1 State of the Heptameric BCS1 Aaa- Atpase within 5.0Å range: probe atom residue distance (Å) B Occ H:Fe301 b:229.6 occ:1.00 FE2 H:FES301 0.0 229.6 1.0 S1 H:FES301 2.2 227.8 1.0 S2 H:FES301 2.2 230.0 1.0 SG H:CYS159 2.3 182.3 1.0 SG H:CYS178 2.3 164.7 1.0 FE1 H:FES301 2.7 233.6 1.0 CB H:CYS159 3.0 180.6 1.0 SG H:CYS164 3.3 177.6 1.0 CB H:CYS178 3.3 159.5 1.0 OG H:SER183 3.5 152.8 1.0 ND1 H:HIS181 3.6 176.7 1.0 CB H:CYS180 3.6 179.4 1.0 SG H:CYS180 3.8 182.9 1.0 N H:HIS181 4.0 172.4 1.0 CE1 H:HIS181 4.4 175.9 1.0 CA H:CYS159 4.4 180.2 1.0 CA H:CYS180 4.5 177.2 1.0 CB H:HIS161 4.6 174.4 1.0 N H:CYS180 4.6 176.4 1.0 CA H:CYS178 4.6 157.2 1.0 CG H:HIS181 4.7 174.9 1.0 ND1 H:HIS161 4.7 176.1 1.0 CB H:SER183 4.7 152.3 1.0 C H:CYS180 4.7 176.9 1.0 CB H:HIS181 4.9 174.0 1.0 CA H:HIS181 4.9 172.2 1.0 C H:CYS178 4.9 158.0 1.0

C.Rosales-Hernandez, M.Thoms, O.Berninghausen, T.Becker, R.Beckmann. Mechanistic Insights Into BCS1-Mediated Mitochondrial Membrane Translocation of the Folded Rieske Protein. Embo J. 2025.
ISSN: ESSN 1460-2075
PubMed: 40410623
DOI: 10.1038/S44318-025-00459-4