Iron in PDB 8q0f: Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm.

All present enzymatic activity of Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm.:
1.6.5.3; 1.6.99.3; 7.1.1.2;

The structure of Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm. also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Potassium	(K)	1 atom
Zinc	(Zn)	2 atoms

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 Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm. (pdb code 8q0f). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 28 binding sites of Iron where determined in the Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm., PDB code: 8q0f:
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 Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm. within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:23.3 occ:1.00 FE1 B:SF4201 0.0 23.3 1.0 SG B:CYS119 2.3 20.8 1.0 S3 B:SF4201 2.3 23.3 1.0 S2 B:SF4201 2.3 23.3 1.0 S4 B:SF4201 2.3 23.3 1.0 FE4 B:SF4201 2.7 23.3 1.0 FE3 B:SF4201 2.7 23.3 1.0 FE2 B:SF4201 2.7 23.3 1.0 CB B:CYS119 3.2 20.8 1.0 S1 B:SF4201 3.9 23.3 1.0 N B:CYS119 4.0 20.8 1.0 CA B:CYS119 4.2 20.8 1.0 OG1 B:THR91 4.2 25.2 1.0 SG B:CYS149 4.5 21.3 1.0 CE2 B:TYR126 4.8 21.0 1.0 CQ2 D:2MR85 4.8 23.6 1.0 SG B:CYS54 4.8 23.7 1.0 SG B:CYS55 4.9 24.4 1.0

Iron binding site 2 out of 28 in the Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm. within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:23.3 occ:1.00 FE2 B:SF4201 0.0 23.3 1.0 SG B:CYS149 2.3 21.3 1.0 S1 B:SF4201 2.3 23.3 1.0 S4 B:SF4201 2.3 23.3 1.0 S3 B:SF4201 2.3 23.3 1.0 FE4 B:SF4201 2.7 23.3 1.0 FE1 B:SF4201 2.7 23.3 1.0 FE3 B:SF4201 2.7 23.3 1.0 CA B:CYS149 3.4 21.3 1.0 CB B:CYS149 3.4 21.3 1.0 C B:CYS149 3.7 21.3 1.0 S2 B:SF4201 3.9 23.3 1.0 NE D:ARG105 4.1 21.0 1.0 O B:CYS149 4.1 21.3 1.0 N B:PRO150 4.2 22.8 1.0 CD2 D:HIS190 4.5 22.7 1.0 NH2 D:ARG105 4.5 21.0 1.0 SG B:CYS55 4.6 24.4 1.0 NE2 D:HIS190 4.6 22.7 1.0 CA B:PRO150 4.7 22.8 1.0 SG B:CYS119 4.7 20.8 1.0 CZ D:ARG105 4.8 21.0 1.0 N B:CYS149 4.8 21.3 1.0 SG B:CYS54 4.8 23.7 1.0 O B:GLY148 4.8 21.9 1.0 CD B:PRO150 4.9 22.8 1.0 CD D:ARG105 4.9 21.0 1.0

Iron binding site 3 out of 28 in the Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm. within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:23.3 occ:1.00 FE3 B:SF4201 0.0 23.3 1.0 SG B:CYS54 2.3 23.7 1.0 S1 B:SF4201 2.3 23.3 1.0 S2 B:SF4201 2.3 23.3 1.0 S4 B:SF4201 2.3 23.3 1.0 FE4 B:SF4201 2.7 23.3 1.0 FE1 B:SF4201 2.7 23.3 1.0 FE2 B:SF4201 2.7 23.3 1.0 CB B:CYS54 3.2 23.7 1.0 CQ2 D:2MR85 3.9 23.6 1.0 S3 B:SF4201 3.9 23.3 1.0 N B:CYS54 3.9 23.7 1.0 NE2 D:HIS190 4.0 22.7 1.0 CA B:CYS54 4.1 23.7 1.0 N B:CYS55 4.2 24.4 1.0 CG D:ARG105 4.4 21.0 1.0 C B:CYS54 4.5 23.7 1.0 CD2 D:HIS190 4.7 22.7 1.0 CB B:ALA53 4.7 25.9 1.0 NE D:ARG105 4.7 21.0 1.0 CD D:ARG105 4.8 21.0 1.0 SG B:CYS119 4.8 20.8 1.0 SG B:CYS55 4.8 24.4 1.0 SG B:CYS149 4.8 21.3 1.0 NH2 D:2MR85 4.9 23.6 1.0 CB D:ARG105 4.9 21.0 1.0 CE1 D:HIS190 5.0 22.7 1.0

Iron binding site 4 out of 28 in the Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm. within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:23.3 occ:1.00 FE4 B:SF4201 0.0 23.3 1.0 SG B:CYS55 2.3 24.4 1.0 S3 B:SF4201 2.3 23.3 1.0 S2 B:SF4201 2.3 23.3 1.0 S1 B:SF4201 2.3 23.3 1.0 FE2 B:SF4201 2.7 23.3 1.0 FE3 B:SF4201 2.7 23.3 1.0 FE1 B:SF4201 2.7 23.3 1.0 CB B:CYS55 3.3 24.4 1.0 N B:CYS55 3.6 24.4 1.0 CA B:CYS55 3.9 24.4 1.0 S4 B:SF4201 3.9 23.3 1.0 CB B:PRO150 4.4 22.8 1.0 CA B:PRO150 4.5 22.8 1.0 C B:CYS54 4.6 23.7 1.0 CA B:GLY117 4.6 22.6 1.0 SG B:CYS54 4.6 23.7 1.0 SG B:CYS119 4.7 20.8 1.0 CB B:CYS54 4.8 23.7 1.0 CA B:CYS149 4.8 21.3 1.0 SG B:CYS149 4.8 21.3 1.0 N B:PRO150 4.8 22.8 1.0 CB B:CYS119 4.9 20.8 1.0 N B:SER118 4.9 20.3 1.0 CA B:GLY90 5.0 25.3 1.0 N B:CYS54 5.0 23.7 1.0

Iron binding site 5 out of 28 in the Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm. within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe301 b:66.6 occ:1.00 FE1 E:FES301 0.0 66.6 1.0 S2 E:FES301 2.2 66.6 1.0 S1 E:FES301 2.2 66.6 1.0 SG E:CYS108 2.3 62.6 1.0 SG E:CYS103 2.3 60.3 1.0 FE2 E:FES301 2.7 66.6 1.0 CB E:CYS108 3.3 62.6 1.0 CB E:CYS103 3.3 60.3 1.0 CA E:CYS144 4.1 58.0 1.0 N E:CYS108 4.1 62.6 1.0 CA E:CYS108 4.3 62.6 1.0 N E:LEU145 4.3 62.0 1.0 O E:ALA147 4.5 65.9 1.0 SG E:CYS144 4.5 58.0 1.0 CB E:CYS144 4.6 58.0 1.0 CA E:CYS103 4.7 60.3 1.0 SG E:CYS148 4.7 65.6 1.0 CG E:MET153 4.7 68.3 1.0 C E:CYS144 4.8 58.0 1.0 C E:CYS103 4.8 60.3 1.0 CA E:CYS148 4.8 65.6 1.0 N E:THR105 4.9 56.5 1.0 CB E:THR105 4.9 56.5 1.0 N E:CYS144 4.9 58.0 1.0 O E:GLU143 4.9 54.3 1.0 CB E:CYS148 5.0 65.6 1.0 O E:THR105 5.0 56.5 1.0

Iron binding site 6 out of 28 in the Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm. within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe301 b:66.6 occ:1.00 FE2 E:FES301 0.0 66.6 1.0 S2 E:FES301 2.2 66.6 1.0 S1 E:FES301 2.2 66.6 1.0 SG E:CYS144 2.3 58.0 1.0 SG E:CYS148 2.3 65.6 1.0 FE1 E:FES301 2.7 66.6 1.0 CB E:CYS144 3.3 58.0 1.0 CB E:CYS148 3.3 65.6 1.0 CA E:CYS144 3.6 58.0 1.0 CA E:CYS148 3.8 65.6 1.0 N E:LEU145 3.9 62.0 1.0 N E:CYS148 4.0 65.6 1.0 N E:GLY146 4.2 62.7 1.0 C E:CYS144 4.2 58.0 1.0 C E:ALA147 4.2 65.9 1.0 N F:GLY103 4.2 60.4 1.0 N E:ALA147 4.3 65.9 1.0 O E:ALA147 4.3 65.9 1.0 SG E:CYS103 4.4 60.3 1.0 SG E:CYS108 4.5 62.6 1.0 CB E:PRO107 4.7 60.6 1.0 CA E:GLY146 4.8 62.7 1.0 CG E:PRO107 4.8 60.6 1.0 C E:GLY146 4.9 62.7 1.0 N E:CYS144 4.9 58.0 1.0 CA F:GLY103 4.9 60.4 1.0 CA E:ALA147 5.0 65.9 1.0 CA F:PRO102 5.0 54.7 1.0 C E:LEU145 5.0 62.0 1.0 CA E:LEU145 5.0 62.0 1.0

Iron binding site 7 out of 28 in the Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm. within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe502 b:32.9 occ:1.00 FE1 F:SF4502 0.0 32.9 1.0 SG F:CYS359 2.3 37.0 1.0 S3 F:SF4502 2.3 32.9 1.0 S4 F:SF4502 2.3 32.9 1.0 S2 F:SF4502 2.3 32.9 1.0 FE3 F:SF4502 2.7 32.9 1.0 FE2 F:SF4502 2.7 32.9 1.0 FE4 F:SF4502 2.7 32.9 1.0 CB F:CYS359 3.3 37.0 1.0 N F:GLN361 3.6 31.7 1.0 N F:GLY360 3.7 33.8 1.0 CB F:GLN361 3.8 31.7 1.0 N F:CYS359 3.8 37.0 1.0 S1 F:SF4502 3.9 32.9 1.0 CA F:CYS359 3.9 37.0 1.0 C F:CYS359 4.0 37.0 1.0 CA F:GLN361 4.3 31.7 1.0 CD F:PRO203 4.4 38.4 1.0 C F:GLY360 4.5 33.8 1.0 CA F:GLY360 4.6 33.8 1.0 N F:CYS362 4.6 30.1 1.0 OE1 F:GLN361 4.7 31.7 1.0 OG F:SER358 4.7 37.7 1.0 SG F:CYS365 4.8 31.9 1.0 SG F:CYS405 4.8 35.4 1.0 O F:CYS359 4.9 37.0 1.0 CD1 F:ILE185 4.9 42.1 1.0 SG F:CYS362 4.9 30.1 1.0 CG F:PRO203 4.9 38.4 1.0 CG F:GLN361 5.0 31.7 1.0 C F:SER358 5.0 37.7 1.0 C F:GLN361 5.0 31.7 1.0

Iron binding site 8 out of 28 in the Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm. within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe502 b:32.9 occ:1.00 FE2 F:SF4502 0.0 32.9 1.0 SG F:CYS365 2.2 31.9 1.0 S1 F:SF4502 2.3 32.9 1.0 S3 F:SF4502 2.3 32.9 1.0 S4 F:SF4502 2.3 32.9 1.0 FE4 F:SF4502 2.7 32.9 1.0 FE3 F:SF4502 2.7 32.9 1.0 FE1 F:SF4502 2.7 32.9 1.0 CB F:CYS365 3.0 31.9 1.0 OG F:SER358 3.3 37.7 1.0 S2 F:SF4502 3.9 32.9 1.0 CA F:CYS365 4.3 31.9 1.0 CB F:SER358 4.4 37.7 1.0 N F:CYS359 4.4 37.0 1.0 N F:GLY360 4.4 33.8 1.0 SG F:CYS362 4.5 30.1 1.0 C F:CYS365 4.6 31.9 1.0 CD2 F:LEU407 4.6 39.9 1.0 CA F:SER358 4.7 37.7 1.0 SG F:CYS405 4.7 35.4 1.0 SG F:CYS359 4.8 37.0 1.0 CB F:LEU407 4.8 39.9 1.0 N F:ARG366 4.8 29.3 1.0 C F:SER358 4.9 37.7 1.0 N F:GLY408 4.9 37.5 1.0 N F:GLN361 5.0 31.7 1.0 O F:CYS365 5.0 31.9 1.0

Iron binding site 9 out of 28 in the Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm. within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe502 b:32.9 occ:1.00 FE3 F:SF4502 0.0 32.9 1.0 S1 F:SF4502 2.3 32.9 1.0 SG F:CYS405 2.3 35.4 1.0 S4 F:SF4502 2.3 32.9 1.0 S2 F:SF4502 2.3 32.9 1.0 FE2 F:SF4502 2.7 32.9 1.0 FE1 F:SF4502 2.7 32.9 1.0 FE4 F:SF4502 2.7 32.9 1.0 CB F:CYS405 3.3 35.4 1.0 S3 F:SF4502 3.9 32.9 1.0 N F:CYS405 4.0 35.4 1.0 CA F:CYS405 4.1 35.4 1.0 CB F:LEU407 4.1 39.9 1.0 CG F:PRO203 4.4 38.4 1.0 CD1 F:ILE185 4.4 42.1 1.0 C F:CYS405 4.4 35.4 1.0 O F:CYS405 4.6 35.4 1.0 N F:LEU407 4.7 39.9 1.0 CD F:PRO203 4.7 38.4 1.0 SG F:CYS365 4.8 31.9 1.0 N F:GLY408 4.8 37.5 1.0 SG F:CYS359 4.8 37.0 1.0 SG F:CYS362 4.8 30.1 1.0 CA F:LEU407 4.9 39.9 1.0

Iron binding site 10 out of 28 in the Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm. within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe502 b:32.9 occ:1.00 FE4 F:SF4502 0.0 32.9 1.0 S3 F:SF4502 2.3 32.9 1.0 S1 F:SF4502 2.3 32.9 1.0 S2 F:SF4502 2.3 32.9 1.0 SG F:CYS362 2.3 30.1 1.0 FE2 F:SF4502 2.7 32.9 1.0 FE1 F:SF4502 2.7 32.9 1.0 FE3 F:SF4502 2.7 32.9 1.0 CB F:CYS362 3.4 30.1 1.0 N F:CYS362 3.6 30.1 1.0 S4 F:SF4502 3.9 32.9 1.0 CA F:CYS362 4.0 30.1 1.0 N F:ILE404 4.3 31.6 1.0 O F:CYS362 4.3 30.1 1.0 CB F:CYS365 4.4 31.9 1.0 CB F:ILE404 4.4 31.6 1.0 CB F:THR403 4.5 31.9 1.0 N F:GLN361 4.5 31.7 1.0 CB F:GLN361 4.5 31.7 1.0 C F:CYS362 4.5 30.1 1.0 SG F:CYS365 4.6 31.9 1.0 C F:GLN361 4.6 31.7 1.0 N F:CYS405 4.7 35.4 1.0 CA F:GLN361 4.8 31.7 1.0 SG F:CYS359 4.8 37.0 1.0 CG2 F:THR403 4.8 31.9 1.0 SG F:CYS405 4.8 35.4 1.0 CG1 F:ILE404 4.8 31.6 1.0 CA F:ILE404 4.9 31.6 1.0 CD1 F:ILE404 4.9 31.6 1.0

D.N.Grba, J.J.Wright, W.Fisher, Z.Yin, J.Hirst. Molecular Mechanism of the Ischemia-Induced Regulatory Switch in Mammalian Complex I Science 2024.
ISSN: ESSN 1095-9203
DOI: 10.1126/SCIENCE.ADO2075