Iron in PDB 8om1: Mitochondrial Complex I From Mus Musculus in the Active State

All present enzymatic activity of Mitochondrial Complex I From Mus Musculus in the Active State:
7.1.1.2;

The structure of Mitochondrial Complex I From Mus Musculus in the Active State also contains other interesting chemical elements:

Sodium	(Na)	1 atom
Zinc	(Zn)	1 atom
Magnesium	(Mg)	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 Mitochondrial Complex I From Mus Musculus in the Active State (pdb code 8om1). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 28 binding sites of Iron where determined in the Mitochondrial Complex I From Mus Musculus in the Active State, PDB code: 8om1:
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 Mitochondrial Complex I From Mus Musculus in the Active State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Mitochondrial Complex I From Mus Musculus in the Active State within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:12.3 occ:1.00 FE1 B:SF4201 0.0 12.3 1.0 SG B:CYS129 2.3 10.6 1.0 S2 B:SF4201 2.3 12.3 1.0 S4 B:SF4201 2.3 12.3 1.0 S3 B:SF4201 2.3 12.3 1.0 FE4 B:SF4201 2.7 12.3 1.0 FE3 B:SF4201 2.8 12.3 1.0 FE2 B:SF4201 2.8 12.3 1.0 CB B:CYS129 3.2 10.6 1.0 O B:HOH357 3.6 9.4 1.0 OG1 B:THR101 3.8 12.0 1.0 O B:HOH334 3.8 9.8 1.0 S1 B:SF4201 3.9 12.3 1.0 N B:CYS129 4.0 10.6 1.0 CA B:CYS129 4.2 10.6 1.0 CQ2 D:2MR85 4.4 12.3 1.0 SG B:CYS159 4.6 10.8 1.0 N B:THR101 4.6 12.0 1.0 CE2 B:TYR136 4.7 10.8 1.0 SG B:CYS64 4.9 12.3 1.0 SG B:CYS65 4.9 12.1 1.0 NH2 D:2MR85 4.9 12.3 1.0 CB B:THR101 5.0 12.0 1.0 CA B:GLY100 5.0 12.4 1.0

Iron binding site 2 out of 28 in the Mitochondrial Complex I From Mus Musculus in the Active State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Mitochondrial Complex I From Mus Musculus in the Active State within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:12.3 occ:1.00 FE2 B:SF4201 0.0 12.3 1.0 S3 B:SF4201 2.3 12.3 1.0 S1 B:SF4201 2.3 12.3 1.0 S4 B:SF4201 2.3 12.3 1.0 SG B:CYS65 2.3 12.1 1.0 FE4 B:SF4201 2.8 12.3 1.0 FE3 B:SF4201 2.8 12.3 1.0 FE1 B:SF4201 2.8 12.3 1.0 CB B:CYS65 3.2 12.1 1.0 O B:HOH334 3.5 9.8 1.0 N B:CYS65 3.6 12.1 1.0 CA B:CYS65 3.7 12.1 1.0 S2 B:SF4201 3.9 12.3 1.0 CA B:PRO160 4.3 12.1 1.0 CB B:PRO160 4.3 12.1 1.0 C B:CYS64 4.5 12.3 1.0 N B:PRO160 4.6 12.1 1.0 CA B:GLY127 4.7 10.9 1.0 CA B:CYS159 4.7 10.8 1.0 CA B:GLY100 4.7 12.4 1.0 SG B:CYS64 4.7 12.3 1.0 CB B:CYS64 4.8 12.3 1.0 SG B:CYS129 4.9 10.6 1.0 C B:CYS159 4.9 10.8 1.0 SG B:CYS159 4.9 10.8 1.0 O B:MET126 4.9 12.3 1.0

Iron binding site 3 out of 28 in the Mitochondrial Complex I From Mus Musculus in the Active State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Mitochondrial Complex I From Mus Musculus in the Active State within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:12.3 occ:1.00 FE3 B:SF4201 0.0 12.3 1.0 SG B:CYS64 2.3 12.3 1.0 S2 B:SF4201 2.3 12.3 1.0 S4 B:SF4201 2.3 12.3 1.0 S1 B:SF4201 2.3 12.3 1.0 FE4 B:SF4201 2.8 12.3 1.0 FE1 B:SF4201 2.8 12.3 1.0 FE2 B:SF4201 2.8 12.3 1.0 CB B:CYS64 3.2 12.3 1.0 CQ2 D:2MR85 3.6 12.3 1.0 NE2 D:HIS190 3.8 12.8 1.0 N B:CYS64 3.9 12.3 1.0 S3 B:SF4201 3.9 12.3 1.0 CA B:CYS64 4.0 12.3 1.0 N B:CYS65 4.1 12.1 1.0 C B:CYS64 4.4 12.3 1.0 CD2 D:HIS190 4.5 12.8 1.0 CG D:ARG105 4.5 11.6 1.0 NH2 D:2MR85 4.8 12.3 1.0 CB B:ALA63 4.8 12.9 1.0 SG B:CYS129 4.8 10.6 1.0 SG B:CYS159 4.9 10.8 1.0 CE1 D:HIS190 4.9 12.8 1.0 SG B:CYS65 4.9 12.1 1.0 NE D:ARG105 5.0 11.6 1.0

Iron binding site 4 out of 28 in the Mitochondrial Complex I From Mus Musculus in the Active State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Mitochondrial Complex I From Mus Musculus in the Active State within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:12.3 occ:1.00 FE4 B:SF4201 0.0 12.3 1.0 S1 B:SF4201 2.3 12.3 1.0 S3 B:SF4201 2.3 12.3 1.0 S2 B:SF4201 2.3 12.3 1.0 SG B:CYS159 2.3 10.8 1.0 FE1 B:SF4201 2.7 12.3 1.0 FE3 B:SF4201 2.8 12.3 1.0 FE2 B:SF4201 2.8 12.3 1.0 CB B:CYS159 3.4 10.8 1.0 CA B:CYS159 3.4 10.8 1.0 C B:CYS159 3.6 10.8 1.0 O B:HOH357 3.8 9.4 1.0 O B:CYS159 3.9 10.8 1.0 S4 B:SF4201 3.9 12.3 1.0 N B:PRO160 4.0 12.1 1.0 NE D:ARG105 4.2 11.6 1.0 CD2 D:HIS190 4.3 12.8 1.0 CA B:PRO160 4.5 12.1 1.0 NE2 D:HIS190 4.5 12.8 1.0 SG B:CYS129 4.7 10.6 1.0 NH1 D:ARG105 4.7 11.6 1.0 CD B:PRO160 4.8 12.1 1.0 N B:CYS159 4.8 10.8 1.0 SG B:CYS65 4.8 12.1 1.0 SG B:CYS64 4.8 12.3 1.0 CZ D:ARG105 4.9 11.6 1.0 O B:GLY158 4.9 11.1 1.0 CD D:ARG105 4.9 11.6 1.0

Iron binding site 5 out of 28 in the Mitochondrial Complex I From Mus Musculus in the Active State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Mitochondrial Complex I From Mus Musculus in the Active State within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe301 b:29.3 occ:1.00 FE1 E:FES301 0.0 29.3 1.0 S1 E:FES301 2.2 29.3 1.0 S2 E:FES301 2.2 29.3 1.0 SG E:CYS103 2.3 29.0 1.0 SG E:CYS108 2.3 29.8 1.0 FE2 E:FES301 2.7 29.3 1.0 CB E:CYS108 3.3 29.8 1.0 CB E:CYS103 3.3 29.0 1.0 N E:CYS108 4.1 29.8 1.0 CA E:CYS144 4.2 27.9 1.0 CA E:CYS108 4.3 29.8 1.0 SD E:MET153 4.3 32.3 1.0 N E:LEU145 4.4 29.2 1.0 SG E:CYS144 4.4 27.9 1.0 CB E:CYS144 4.5 27.9 1.0 CA E:CYS103 4.6 29.0 1.0 SG E:CYS148 4.7 30.1 1.0 CA E:CYS148 4.7 30.1 1.0 CB E:THR105 4.8 27.4 1.0 C E:CYS103 4.8 29.0 1.0 CB E:CYS148 4.9 30.1 1.0 C E:CYS144 4.9 27.9 1.0 N E:THR105 4.9 27.4 1.0 CG E:MET153 4.9 32.3 1.0 O E:THR105 4.9 27.4 1.0 OG1 E:THR105 5.0 27.4 1.0

Iron binding site 6 out of 28 in the Mitochondrial Complex I From Mus Musculus in the Active State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Mitochondrial Complex I From Mus Musculus in the Active State within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe301 b:29.3 occ:1.00 FE2 E:FES301 0.0 29.3 1.0 S2 E:FES301 2.2 29.3 1.0 S1 E:FES301 2.2 29.3 1.0 SG E:CYS144 2.3 27.9 1.0 SG E:CYS148 2.3 30.1 1.0 FE1 E:FES301 2.7 29.3 1.0 CB E:CYS144 3.3 27.9 1.0 CB E:CYS148 3.3 30.1 1.0 CA E:CYS144 3.8 27.9 1.0 CA E:CYS148 3.8 30.1 1.0 N E:CYS148 3.8 30.1 1.0 N E:GLY146 4.1 29.2 1.0 N E:LEU145 4.1 29.2 1.0 N E:ALA147 4.1 30.6 1.0 C E:CYS144 4.3 27.9 1.0 N F:GLY103 4.3 28.8 1.0 SG E:CYS103 4.3 29.0 1.0 C E:ALA147 4.5 30.6 1.0 CA E:GLY146 4.6 29.2 1.0 SG E:CYS108 4.6 29.8 1.0 CA F:PRO102 4.8 27.0 1.0 CB E:PRO107 4.8 29.1 1.0 C E:GLY146 4.8 29.2 1.0 CG E:PRO107 4.9 29.1 1.0 CA E:ALA147 5.0 30.6 1.0 C E:LEU145 5.0 29.2 1.0

Iron binding site 7 out of 28 in the Mitochondrial Complex I From Mus Musculus in the Active State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Mitochondrial Complex I From Mus Musculus in the Active State within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe501 b:17.7 occ:1.00 FE1 F:SF4501 0.0 17.7 1.0 S3 F:SF4501 2.3 17.7 1.0 S4 F:SF4501 2.3 17.7 1.0 SG F:CYS362 2.3 15.4 1.0 S2 F:SF4501 2.3 17.7 1.0 FE2 F:SF4501 2.7 17.7 1.0 FE4 F:SF4501 2.8 17.7 1.0 FE3 F:SF4501 2.8 17.7 1.0 CB F:CYS362 3.4 15.4 1.0 N F:CYS362 3.7 15.4 1.0 S1 F:SF4501 3.9 17.7 1.0 CB F:CYS365 4.1 16.2 1.0 CA F:CYS362 4.1 15.4 1.0 N F:ILE404 4.2 16.9 1.0 O F:CYS362 4.3 15.4 1.0 CB F:ILE404 4.3 16.9 1.0 CB F:THR403 4.5 17.0 1.0 SG F:CYS365 4.5 16.2 1.0 C F:CYS362 4.6 15.4 1.0 N F:CYS405 4.6 18.3 1.0 CG1 F:ILE404 4.8 16.9 1.0 CB F:GLN361 4.8 17.2 1.0 SG F:CYS359 4.8 18.1 1.0 CD1 F:ILE404 4.8 16.9 1.0 CA F:ILE404 4.8 16.9 1.0 C F:GLN361 4.8 17.2 1.0 CG2 F:THR403 4.9 17.0 1.0 N F:GLN361 4.9 17.2 1.0 SG F:CYS405 4.9 18.3 1.0

Iron binding site 8 out of 28 in the Mitochondrial Complex I From Mus Musculus in the Active State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Mitochondrial Complex I From Mus Musculus in the Active State within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe501 b:17.7 occ:1.00 FE2 F:SF4501 0.0 17.7 1.0 SG F:CYS365 2.2 16.2 1.0 S4 F:SF4501 2.3 17.7 1.0 S1 F:SF4501 2.3 17.7 1.0 S3 F:SF4501 2.3 17.7 1.0 FE1 F:SF4501 2.7 17.7 1.0 FE3 F:SF4501 2.7 17.7 1.0 FE4 F:SF4501 2.8 17.7 1.0 CB F:CYS365 3.0 16.2 1.0 OG F:SER358 3.7 19.3 1.0 S2 F:SF4501 3.9 17.7 1.0 CD2 F:LEU407 4.1 20.7 1.0 CB F:SER358 4.3 19.3 1.0 N F:CYS359 4.3 18.1 1.0 CA F:CYS365 4.4 16.2 1.0 CB F:LEU407 4.4 20.7 1.0 CA F:SER358 4.5 19.3 1.0 SG F:CYS362 4.6 15.4 1.0 N F:GLY408 4.6 19.8 1.0 SG F:CYS405 4.7 18.3 1.0 C F:CYS365 4.7 16.2 1.0 CG F:LEU407 4.7 20.7 1.0 SG F:CYS359 4.9 18.1 1.0 N F:GLY360 4.9 17.1 1.0 C F:SER358 4.9 19.3 1.0 N F:ARG366 5.0 16.5 1.0

Iron binding site 9 out of 28 in the Mitochondrial Complex I From Mus Musculus in the Active State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Mitochondrial Complex I From Mus Musculus in the Active State within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe501 b:17.7 occ:1.00 FE3 F:SF4501 0.0 17.7 1.0 S4 F:SF4501 2.3 17.7 1.0 S1 F:SF4501 2.3 17.7 1.0 SG F:CYS405 2.3 18.3 1.0 S2 F:SF4501 2.3 17.7 1.0 FE2 F:SF4501 2.7 17.7 1.0 FE4 F:SF4501 2.7 17.7 1.0 FE1 F:SF4501 2.8 17.7 1.0 CB F:CYS405 3.3 18.3 1.0 N F:CYS405 3.9 18.3 1.0 S3 F:SF4501 3.9 17.7 1.0 CA F:CYS405 4.0 18.3 1.0 CB F:LEU407 4.1 20.7 1.0 CG F:PRO203 4.1 19.8 1.0 C F:CYS405 4.3 18.3 1.0 O F:CYS405 4.3 18.3 1.0 CD1 F:ILE185 4.3 21.3 1.0 CD F:PRO203 4.5 19.8 1.0 N F:LEU407 4.7 20.7 1.0 SG F:CYS359 4.7 18.1 1.0 N F:GLY408 4.8 19.8 1.0 SG F:CYS365 4.8 16.2 1.0 SG F:CYS362 4.9 15.4 1.0 CA F:LEU407 4.9 20.7 1.0 C F:ILE404 5.0 16.9 1.0

Iron binding site 10 out of 28 in the Mitochondrial Complex I From Mus Musculus in the Active State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Mitochondrial Complex I From Mus Musculus in the Active State within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe501 b:17.7 occ:1.00 FE4 F:SF4501 0.0 17.7 1.0 SG F:CYS359 2.3 18.1 1.0 S3 F:SF4501 2.3 17.7 1.0 S2 F:SF4501 2.3 17.7 1.0 S1 F:SF4501 2.3 17.7 1.0 FE3 F:SF4501 2.7 17.7 1.0 FE1 F:SF4501 2.8 17.7 1.0 FE2 F:SF4501 2.8 17.7 1.0 CB F:CYS359 3.3 18.1 1.0 N F:CYS359 3.7 18.1 1.0 N F:GLN361 3.8 17.2 1.0 CA F:CYS359 3.9 18.1 1.0 N F:GLY360 3.9 17.1 1.0 S4 F:SF4501 3.9 17.7 1.0 CB F:GLN361 4.0 17.2 1.0 C F:CYS359 4.2 18.1 1.0 CD F:PRO203 4.2 19.8 1.0 CA F:GLN361 4.5 17.2 1.0 N F:CYS362 4.5 15.4 1.0 NE2 F:GLN361 4.5 17.2 1.0 OG F:SER358 4.7 19.3 1.0 C F:GLY360 4.7 17.1 1.0 CG F:PRO203 4.8 19.8 1.0 SG F:CYS405 4.8 18.3 1.0 C F:SER358 4.8 19.3 1.0 SG F:CYS365 4.8 16.2 1.0 CA F:GLY360 4.8 17.1 1.0 SG F:CYS362 4.9 15.4 1.0 CG1 F:ILE185 5.0 21.3 1.0

D.N.Grba, I.Chung, H.R.Bridges, A.A.Agip, J.Hirst. Investigation of Hydrated Channels and Proton Pathways in A High-Resolution Cryo-Em Structure of Mammalian Complex I. Sci Adv V. 9 I1359 2023.
ISSN: ESSN 2375-2548
PubMed: 37531432
DOI: 10.1126/SCIADV.ADI1359