Iron in PDB 7ak5: Cryo-Em Structure of Respiratory Complex I in the Deactive State From Mus Musculus at 3.2 A

All present enzymatic activity of Cryo-Em Structure of Respiratory Complex I in the Deactive State From Mus Musculus at 3.2 A:
7.1.1.2;

The structure of Cryo-Em Structure of Respiratory Complex I in the Deactive State From Mus Musculus at 3.2 A also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 28;

Binding sites:

The binding sites of Iron atom in the Cryo-Em Structure of Respiratory Complex I in the Deactive State From Mus Musculus at 3.2 A (pdb code 7ak5). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 28 binding sites of Iron where determined in the Cryo-Em Structure of Respiratory Complex I in the Deactive State From Mus Musculus at 3.2 A, PDB code: 7ak5:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 28 in the Cryo-Em Structure of Respiratory Complex I in the Deactive State From Mus Musculus at 3.2 A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cryo-Em Structure of Respiratory Complex I in the Deactive State From Mus Musculus at 3.2 A within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:14.7 occ:1.00 FE1 B:SF4201 0.0 14.7 1.0 SG B:CYS129 2.3 14.7 1.0 S2 B:SF4201 2.3 14.7 1.0 S3 B:SF4201 2.3 14.7 1.0 S4 B:SF4201 2.3 14.7 1.0 FE4 B:SF4201 2.7 14.7 1.0 FE3 B:SF4201 2.7 14.7 1.0 FE2 B:SF4201 2.7 14.7 1.0 CB B:CYS129 3.2 14.7 1.0 S1 B:SF4201 3.9 14.7 1.0 N B:CYS129 4.0 14.7 1.0 OG1 B:THR101 4.1 18.8 1.0 CQ2 D:2MR85 4.2 18.9 1.0 CA B:CYS129 4.2 14.7 1.0 SG B:CYS159 4.7 13.1 1.0 SG B:CYS64 4.7 17.1 1.0 SG B:CYS65 4.8 17.6 1.0 N B:THR101 4.8 18.8 1.0 CA B:GLY100 4.9 18.6 1.0

Iron binding site 2 out of 28 in the Cryo-Em Structure of Respiratory Complex I in the Deactive State From Mus Musculus at 3.2 A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cryo-Em Structure of Respiratory Complex I in the Deactive State From Mus Musculus at 3.2 A within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:14.7 occ:1.00 FE2 B:SF4201 0.0 14.7 1.0 SG B:CYS65 2.3 17.6 1.0 S4 B:SF4201 2.3 14.7 1.0 S3 B:SF4201 2.3 14.7 1.0 S1 B:SF4201 2.3 14.7 1.0 FE3 B:SF4201 2.7 14.7 1.0 FE4 B:SF4201 2.7 14.7 1.0 FE1 B:SF4201 2.7 14.7 1.0 CB B:CYS65 3.2 17.6 1.0 N B:CYS65 3.7 17.6 1.0 CA B:CYS65 3.8 17.6 1.0 S2 B:SF4201 3.9 14.7 1.0 C B:CYS64 4.1 17.1 1.0 O B:CYS64 4.4 17.1 1.0 CA B:PRO160 4.4 14.5 1.0 CB B:PRO160 4.4 14.5 1.0 CA B:CYS159 4.4 13.1 1.0 O B:GLY158 4.4 12.9 1.0 CA B:GLY127 4.6 14.4 1.0 SG B:CYS64 4.7 17.1 1.0 SG B:CYS159 4.8 13.1 1.0 N B:PRO160 4.8 14.5 1.0 SG B:CYS129 4.8 14.7 1.0 C B:CYS159 4.9 13.1 1.0 N B:SER128 5.0 13.2 1.0

Iron binding site 3 out of 28 in the Cryo-Em Structure of Respiratory Complex I in the Deactive State From Mus Musculus at 3.2 A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Cryo-Em Structure of Respiratory Complex I in the Deactive State From Mus Musculus at 3.2 A within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:14.7 occ:1.00 FE3 B:SF4201 0.0 14.7 1.0 SG B:CYS64 2.2 17.1 1.0 S1 B:SF4201 2.3 14.7 1.0 S4 B:SF4201 2.3 14.7 1.0 S2 B:SF4201 2.3 14.7 1.0 FE2 B:SF4201 2.7 14.7 1.0 FE4 B:SF4201 2.7 14.7 1.0 FE1 B:SF4201 2.7 14.7 1.0 CB B:CYS64 3.3 17.1 1.0 C B:CYS64 3.8 17.1 1.0 CA B:CYS64 3.8 17.1 1.0 S3 B:SF4201 3.9 14.7 1.0 N B:CYS64 3.9 17.1 1.0 N B:CYS65 4.0 17.6 1.0 NE2 D:HIS190 4.0 14.9 1.0 CQ2 D:2MR85 4.1 18.9 1.0 O B:CYS64 4.3 17.1 1.0 CG D:ARG105 4.6 14.3 1.0 CD2 D:HIS190 4.7 14.9 1.0 SG B:CYS65 4.7 17.6 1.0 SG B:CYS129 4.8 14.7 1.0 SG B:CYS159 4.8 13.1 1.0 CB B:ALA63 4.8 19.4 1.0 NH2 D:2MR85 4.9 18.9 1.0 C B:ALA63 4.9 19.4 1.0 CA B:CYS65 5.0 17.6 1.0 CB B:CYS65 5.0 17.6 1.0

Iron binding site 4 out of 28 in the Cryo-Em Structure of Respiratory Complex I in the Deactive State From Mus Musculus at 3.2 A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Cryo-Em Structure of Respiratory Complex I in the Deactive State From Mus Musculus at 3.2 A within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:14.7 occ:1.00 FE4 B:SF4201 0.0 14.7 1.0 SG B:CYS159 2.3 13.1 1.0 S2 B:SF4201 2.3 14.7 1.0 S1 B:SF4201 2.3 14.7 1.0 S3 B:SF4201 2.3 14.7 1.0 FE3 B:SF4201 2.7 14.7 1.0 FE1 B:SF4201 2.7 14.7 1.0 FE2 B:SF4201 2.7 14.7 1.0 CB B:CYS159 3.2 13.1 1.0 CA B:CYS159 3.4 13.1 1.0 C B:CYS159 3.8 13.1 1.0 S4 B:SF4201 3.9 14.7 1.0 O B:CYS159 4.2 13.1 1.0 N B:PRO160 4.4 14.5 1.0 NE D:ARG105 4.4 14.3 1.0 CD2 D:HIS190 4.4 14.9 1.0 NE2 D:HIS190 4.6 14.9 1.0 NH1 D:ARG105 4.7 14.3 1.0 N B:CYS159 4.7 13.1 1.0 SG B:CYS129 4.7 14.7 1.0 SG B:CYS64 4.7 17.1 1.0 O B:GLY158 4.7 12.9 1.0 CA B:PRO160 4.8 14.5 1.0 SG B:CYS65 4.8 17.6 1.0 CG D:ARG105 4.9 14.3 1.0

Iron binding site 5 out of 28 in the Cryo-Em Structure of Respiratory Complex I in the Deactive State From Mus Musculus at 3.2 A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Cryo-Em Structure of Respiratory Complex I in the Deactive State From Mus Musculus at 3.2 A within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe301 b:65.8 occ:1.00 FE1 E:FES301 0.0 65.8 1.0 S2 E:FES301 2.2 65.8 1.0 S1 E:FES301 2.2 65.8 1.0 SG E:CYS103 2.3 60.9 1.0 SG E:CYS108 2.3 62.9 1.0 FE2 E:FES301 2.7 65.8 1.0 CB E:CYS103 3.3 60.9 1.0 CB E:CYS108 3.4 62.9 1.0 CA E:CYS144 4.3 56.2 1.0 N E:CYS108 4.3 62.9 1.0 CA E:CYS108 4.5 62.9 1.0 CB E:THR105 4.5 57.5 1.0 CA E:CYS148 4.6 67.8 1.0 O E:ALA151 4.6 69.0 1.0 CA E:CYS103 4.6 60.9 1.0 SG E:CYS144 4.6 56.2 1.0 SG E:CYS148 4.7 67.8 1.0 N E:LEU145 4.7 59.7 1.0 O E:THR105 4.8 57.5 1.0 CB E:CYS144 4.8 56.2 1.0 C E:CYS103 4.8 60.9 1.0 O E:CYS103 4.8 60.9 1.0 N E:CYS148 4.9 67.8 1.0 N E:THR105 4.9 57.5 1.0

Iron binding site 6 out of 28 in the Cryo-Em Structure of Respiratory Complex I in the Deactive State From Mus Musculus at 3.2 A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Cryo-Em Structure of Respiratory Complex I in the Deactive State From Mus Musculus at 3.2 A within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe301 b:65.8 occ:1.00 FE2 E:FES301 0.0 65.8 1.0 S2 E:FES301 2.2 65.8 1.0 S1 E:FES301 2.2 65.8 1.0 SG E:CYS148 2.3 67.8 1.0 SG E:CYS144 2.3 56.2 1.0 FE1 E:FES301 2.7 65.8 1.0 CB E:CYS144 3.3 56.2 1.0 CB E:CYS148 3.3 67.8 1.0 CA E:CYS148 3.5 67.8 1.0 CA E:CYS144 3.6 56.2 1.0 N E:CYS148 3.6 67.8 1.0 N E:LEU145 3.9 59.7 1.0 SG E:CYS103 4.2 60.9 1.0 C E:CYS144 4.3 56.2 1.0 N F:GLY103 4.3 61.5 1.0 N E:GLY146 4.4 61.9 1.0 N E:ALA147 4.5 65.3 1.0 C E:ALA147 4.5 65.3 1.0 SG E:CYS108 4.5 62.9 1.0 CA F:PRO102 4.6 54.5 1.0 N E:CYS144 4.8 56.2 1.0

Iron binding site 7 out of 28 in the Cryo-Em Structure of Respiratory Complex I in the Deactive State From Mus Musculus at 3.2 A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Cryo-Em Structure of Respiratory Complex I in the Deactive State From Mus Musculus at 3.2 A within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe502 b:31.8 occ:1.00 FE1 F:SF4502 0.0 31.8 1.0 SG F:CYS362 2.2 27.3 1.0 S2 F:SF4502 2.3 31.8 1.0 S4 F:SF4502 2.3 31.8 1.0 S3 F:SF4502 2.3 31.8 1.0 FE4 F:SF4502 2.7 31.8 1.0 FE3 F:SF4502 2.7 31.8 1.0 FE2 F:SF4502 2.7 31.8 1.0 CB F:CYS362 3.0 27.3 1.0 N F:CYS362 3.8 27.3 1.0 S1 F:SF4502 3.9 31.8 1.0 CA F:CYS362 4.0 27.3 1.0 CB F:ILE404 4.2 29.9 1.0 N F:ILE404 4.4 29.9 1.0 CG F:GLN361 4.4 29.3 1.0 CB F:CYS365 4.5 29.0 1.0 N F:CYS405 4.6 34.6 1.0 SG F:CYS359 4.6 33.7 1.0 CD1 F:ILE404 4.6 29.9 1.0 CG1 F:ILE404 4.7 29.9 1.0 SG F:CYS365 4.7 29.0 1.0 SG F:CYS405 4.8 34.6 1.0 CA F:ILE404 4.8 29.9 1.0

Iron binding site 8 out of 28 in the Cryo-Em Structure of Respiratory Complex I in the Deactive State From Mus Musculus at 3.2 A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Cryo-Em Structure of Respiratory Complex I in the Deactive State From Mus Musculus at 3.2 A within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe502 b:31.8 occ:1.00 FE2 F:SF4502 0.0 31.8 1.0 SG F:CYS365 2.3 29.0 1.0 S3 F:SF4502 2.3 31.8 1.0 S1 F:SF4502 2.3 31.8 1.0 S4 F:SF4502 2.3 31.8 1.0 FE1 F:SF4502 2.7 31.8 1.0 FE3 F:SF4502 2.7 31.8 1.0 FE4 F:SF4502 2.7 31.8 1.0 CB F:CYS365 3.0 29.0 1.0 OG F:SER358 3.4 35.7 1.0 S2 F:SF4502 3.9 31.8 1.0 CA F:CYS365 4.5 29.0 1.0 CB F:SER358 4.5 35.7 1.0 CB F:CYS362 4.6 27.3 1.0 N F:CYS359 4.6 33.7 1.0 SG F:CYS362 4.7 27.3 1.0 SG F:CYS405 4.7 34.6 1.0 CD2 F:LEU407 4.7 39.9 1.0 SG F:CYS359 4.8 33.7 1.0 CB F:LEU407 4.8 39.9 1.0 CA F:SER358 4.8 35.7 1.0 N F:ARG366 5.0 25.9 1.0

Iron binding site 9 out of 28 in the Cryo-Em Structure of Respiratory Complex I in the Deactive State From Mus Musculus at 3.2 A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Cryo-Em Structure of Respiratory Complex I in the Deactive State From Mus Musculus at 3.2 A within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe502 b:31.8 occ:1.00 FE3 F:SF4502 0.0 31.8 1.0 SG F:CYS405 2.3 34.6 1.0 S4 F:SF4502 2.3 31.8 1.0 S2 F:SF4502 2.3 31.8 1.0 S1 F:SF4502 2.3 31.8 1.0 FE1 F:SF4502 2.7 31.8 1.0 FE2 F:SF4502 2.7 31.8 1.0 FE4 F:SF4502 2.7 31.8 1.0 CB F:CYS405 3.3 34.6 1.0 S3 F:SF4502 3.9 31.8 1.0 CD1 F:ILE185 3.9 40.2 1.0 N F:CYS405 4.0 34.6 1.0 CB F:LEU407 4.1 39.9 1.0 CA F:CYS405 4.2 34.6 1.0 CG F:PRO203 4.6 35.8 1.0 C F:CYS405 4.6 34.6 1.0 N F:LEU407 4.7 39.9 1.0 SG F:CYS362 4.8 27.3 1.0 SG F:CYS365 4.8 29.0 1.0 SG F:CYS359 4.9 33.7 1.0 CG1 F:ILE185 4.9 40.2 1.0

Iron binding site 10 out of 28 in the Cryo-Em Structure of Respiratory Complex I in the Deactive State From Mus Musculus at 3.2 A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Cryo-Em Structure of Respiratory Complex I in the Deactive State From Mus Musculus at 3.2 A within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe502 b:31.8 occ:1.00 FE4 F:SF4502 0.0 31.8 1.0 SG F:CYS359 2.3 33.7 1.0 S3 F:SF4502 2.3 31.8 1.0 S2 F:SF4502 2.3 31.8 1.0 S1 F:SF4502 2.3 31.8 1.0 FE1 F:SF4502 2.7 31.8 1.0 FE2 F:SF4502 2.7 31.8 1.0 FE3 F:SF4502 2.7 31.8 1.0 CB F:CYS359 3.3 33.7 1.0 N F:CYS359 3.7 33.7 1.0 S4 F:SF4502 3.9 31.8 1.0 N F:GLY360 3.9 29.9 1.0 CA F:CYS359 4.0 33.7 1.0 C F:CYS359 4.4 33.7 1.0 CD F:PRO203 4.4 35.8 1.0 CG F:GLN361 4.5 29.3 1.0 CD1 F:ILE185 4.5 40.2 1.0 OG F:SER358 4.5 35.7 1.0 N F:GLN361 4.6 29.3 1.0 SG F:CYS362 4.7 27.3 1.0 CG1 F:ILE185 4.8 40.2 1.0 SG F:CYS365 4.8 29.0 1.0 SG F:CYS405 4.9 34.6 1.0 CG F:PRO203 4.9 35.8 1.0 C F:SER358 4.9 35.7 1.0 NE2 F:GLN361 4.9 29.3 1.0 N F:CYS362 5.0 27.3 1.0

Z.Yin, N.Burger, D.Kula-Alwar, D.Aksentijevic, H.R.Bridges, H.Prag, D.Grba, C.Viscomi, A.James, A.Mottahedin, T.Krieg, M.P.Murphy, J.Hirst. Structural Basis For A Complex I Mutation That Blocks Pathological Ros Production To Be Published.
DOI: 10.1038/S41467-021-20942-W