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Iron in PDB 8q0a: Inward-Facing, Closed Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm.

Enzymatic activity of Inward-Facing, Closed Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm.

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

Other elements in 8q0a:

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

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

Iron Binding Sites:

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, Closed Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm. (pdb code 8q0a). 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, Closed Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm., PDB code: 8q0a:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 28 in 8q0a

Go back to Iron Binding Sites List in 8q0a
Iron binding site 1 out of 28 in the Inward-Facing, Closed 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, Closed 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:24.4
occ:1.00
 FE1 B:SF4201 0.0 24.4 1.0
SG B:CYS119 2.2 20.7 1.0
S2 B:SF4201 2.3 24.4 1.0
S3 B:SF4201 2.3 24.4 1.0
S4 B:SF4201 2.3 24.4 1.0
FE4 B:SF4201 2.7 24.4 1.0
FE3 B:SF4201 2.7 24.4 1.0
FE2 B:SF4201 2.7 24.4 1.0
CB B:CYS119 3.2 20.7 1.0
N B:CYS119 3.9 20.7 1.0
S1 B:SF4201 3.9 24.4 1.0
CA B:CYS119 4.1 20.7 1.0
OG1 B:THR91 4.2 23.5 1.0
SG B:CYS149 4.3 20.7 1.0
CQ2 D:2MR85 4.6 24.0 1.0
SG B:CYS54 4.8 24.4 1.0
SG B:CYS55 4.9 23.6 1.0
CE1 B:TYR126 4.9 21.0 1.0
N B:THR91 5.0 23.5 1.0

Iron binding site 2 out of 28 in 8q0a

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Iron binding site 2 out of 28 in the Inward-Facing, Closed 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, Closed 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:24.4
occ:1.00
 FE2 B:SF4201 0.0 24.4 1.0
SG B:CYS149 2.2 20.7 1.0
S1 B:SF4201 2.3 24.4 1.0
S3 B:SF4201 2.3 24.4 1.0
S4 B:SF4201 2.3 24.4 1.0
FE4 B:SF4201 2.7 24.4 1.0
FE1 B:SF4201 2.7 24.4 1.0
FE3 B:SF4201 2.7 24.4 1.0
CB B:CYS149 3.3 20.7 1.0
CA B:CYS149 3.3 20.7 1.0
C B:CYS149 3.7 20.7 1.0
S2 B:SF4201 3.9 24.4 1.0
N B:PRO150 4.1 23.0 1.0
O B:CYS149 4.3 20.7 1.0
SG B:CYS55 4.3 23.6 1.0
CA B:PRO150 4.4 23.0 1.0
NE D:ARG105 4.5 22.4 1.0
O B:GLY148 4.6 20.9 1.0
CD2 D:HIS190 4.6 23.8 1.0
NE2 D:HIS190 4.7 23.8 1.0
N B:CYS149 4.7 20.7 1.0
SG B:CYS119 4.7 20.7 1.0
SG B:CYS54 4.8 24.4 1.0
CB B:PRO150 4.9 23.0 1.0
CD B:PRO150 4.9 23.0 1.0
NH2 D:ARG105 4.9 22.4 1.0
N B:SER118 5.0 20.2 1.0

Iron binding site 3 out of 28 in 8q0a

Go back to Iron Binding Sites List in 8q0a
Iron binding site 3 out of 28 in the Inward-Facing, Closed 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, Closed 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:24.4
occ:1.00
 FE3 B:SF4201 0.0 24.4 1.0
SG B:CYS54 2.3 24.4 1.0
S4 B:SF4201 2.3 24.4 1.0
S1 B:SF4201 2.3 24.4 1.0
S2 B:SF4201 2.3 24.4 1.0
FE4 B:SF4201 2.7 24.4 1.0
FE1 B:SF4201 2.7 24.4 1.0
FE2 B:SF4201 2.7 24.4 1.0
CB B:CYS54 3.2 24.4 1.0
CQ2 D:2MR85 3.8 24.0 1.0
S3 B:SF4201 3.9 24.4 1.0
N B:CYS54 4.0 24.4 1.0
NE2 D:HIS190 4.0 23.8 1.0
CA B:CYS54 4.1 24.4 1.0
N B:CYS55 4.2 23.6 1.0
CG D:ARG105 4.4 22.4 1.0
C B:CYS54 4.5 24.4 1.0
SG B:CYS149 4.6 20.7 1.0
NE D:ARG105 4.7 22.4 1.0
SG B:CYS119 4.8 20.7 1.0
CB B:ALA53 4.8 24.6 1.0
SG B:CYS55 4.8 23.6 1.0
CD D:ARG105 4.8 22.4 1.0
CD2 D:HIS190 4.8 23.8 1.0
CE1 D:HIS190 4.9 23.8 1.0
NH2 D:2MR85 4.9 24.0 1.0

Iron binding site 4 out of 28 in 8q0a

Go back to Iron Binding Sites List in 8q0a
Iron binding site 4 out of 28 in the Inward-Facing, Closed 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, Closed 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:24.4
occ:1.00
 FE4 B:SF4201 0.0 24.4 1.0
SG B:CYS55 2.3 23.6 1.0
S3 B:SF4201 2.3 24.4 1.0
S2 B:SF4201 2.3 24.4 1.0
S1 B:SF4201 2.3 24.4 1.0
FE2 B:SF4201 2.7 24.4 1.0
FE3 B:SF4201 2.7 24.4 1.0
FE1 B:SF4201 2.7 24.4 1.0
CB B:CYS55 3.2 23.6 1.0
N B:CYS55 3.5 23.6 1.0
CA B:CYS55 3.8 23.6 1.0
S4 B:SF4201 3.9 24.4 1.0
CA B:GLY90 4.3 23.6 1.0
C B:CYS54 4.5 24.4 1.0
SG B:CYS54 4.6 24.4 1.0
CA B:GLY117 4.7 21.1 1.0
CB B:CYS54 4.7 24.4 1.0
N B:GLY90 4.7 23.6 1.0
SG B:CYS119 4.7 20.7 1.0
N B:CYS54 4.8 24.4 1.0
CA B:PRO150 4.8 23.0 1.0
CB B:PRO150 4.8 23.0 1.0
CB B:CYS119 4.9 20.7 1.0
SG B:CYS149 4.9 20.7 1.0
CA B:CYS54 4.9 24.4 1.0
N B:SER118 4.9 20.2 1.0

Iron binding site 5 out of 28 in 8q0a

Go back to Iron Binding Sites List in 8q0a
Iron binding site 5 out of 28 in the Inward-Facing, Closed 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, Closed 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:59.8
occ:1.00
 FE1 E:FES301 0.0 59.8 1.0
S1 E:FES301 2.2 59.8 1.0
S2 E:FES301 2.2 59.8 1.0
SG E:CYS108 2.2 56.8 1.0
SG E:CYS103 2.3 57.6 1.0
FE2 E:FES301 2.7 59.8 1.0
CB E:CYS108 3.2 56.8 1.0
CB E:CYS103 3.4 57.6 1.0
CA E:CYS144 4.1 54.7 1.0
N E:CYS108 4.2 56.8 1.0
N E:LEU145 4.3 57.0 1.0
CA E:CYS108 4.3 56.8 1.0
SG E:CYS144 4.5 54.7 1.0
SD E:MET153 4.5 61.5 1.0
CB E:CYS144 4.6 54.7 1.0
CA E:CYS103 4.7 57.6 1.0
CA E:CYS148 4.7 58.8 1.0
C E:CYS144 4.7 54.7 1.0
SG E:CYS148 4.8 58.8 1.0
CB E:THR105 4.9 52.9 1.0
N E:THR105 4.9 52.9 1.0
C E:CYS103 4.9 57.6 1.0
N E:CYS144 4.9 54.7 1.0
O E:GLU143 4.9 52.0 1.0
CG E:MET153 5.0 61.5 1.0
O E:ALA147 5.0 59.9 1.0

Iron binding site 6 out of 28 in 8q0a

Go back to Iron Binding Sites List in 8q0a
Iron binding site 6 out of 28 in the Inward-Facing, Closed 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, Closed 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:59.8
occ:1.00
 FE2 E:FES301 0.0 59.8 1.0
S2 E:FES301 2.2 59.8 1.0
S1 E:FES301 2.2 59.8 1.0
SG E:CYS144 2.3 54.7 1.0
SG E:CYS148 2.3 58.8 1.0
FE1 E:FES301 2.7 59.8 1.0
CB E:CYS144 3.3 54.7 1.0
CB E:CYS148 3.3 58.8 1.0
CA E:CYS148 3.6 58.8 1.0
CA E:CYS144 3.6 54.7 1.0
N E:CYS148 3.8 58.8 1.0
N E:LEU145 3.9 57.0 1.0
N E:GLY146 4.0 57.5 1.0
C E:CYS144 4.2 54.7 1.0
N F:GLY103 4.3 55.9 1.0
SG E:CYS103 4.4 57.6 1.0
C E:ALA147 4.4 59.9 1.0
N E:ALA147 4.5 59.9 1.0
SG E:CYS108 4.5 56.8 1.0
CA E:GLY146 4.6 57.5 1.0
C E:GLY146 4.7 57.5 1.0
CB E:PRO107 4.8 54.4 1.0
CG E:PRO107 4.8 54.4 1.0
O E:ALA147 4.9 59.9 1.0
N E:CYS144 4.9 54.7 1.0
C E:LEU145 4.9 57.0 1.0
CA F:PRO102 5.0 52.6 1.0
CA E:LEU145 5.0 57.0 1.0

Iron binding site 7 out of 28 in 8q0a

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Iron binding site 7 out of 28 in the Inward-Facing, Closed 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, Closed 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:37.9
occ:1.00
 FE1 F:SF4502 0.0 37.9 1.0
SG F:CYS359 2.3 37.7 1.0
S3 F:SF4502 2.3 37.9 1.0
S2 F:SF4502 2.3 37.9 1.0
S4 F:SF4502 2.3 37.9 1.0
FE2 F:SF4502 2.7 37.9 1.0
FE4 F:SF4502 2.7 37.9 1.0
FE3 F:SF4502 2.7 37.9 1.0
CB F:CYS359 3.3 37.7 1.0
N F:GLY360 3.7 34.2 1.0
N F:GLN361 3.8 34.1 1.0
N F:CYS359 3.9 37.7 1.0
S1 F:SF4502 3.9 37.9 1.0
CA F:CYS359 4.0 37.7 1.0
C F:CYS359 4.2 37.7 1.0
CB F:GLN361 4.2 34.1 1.0
CD F:PRO203 4.4 39.7 1.0
N F:CYS362 4.5 33.1 1.0
CA F:GLN361 4.6 34.1 1.0
C F:GLY360 4.6 34.2 1.0
CA F:GLY360 4.6 34.2 1.0
SG F:CYS365 4.8 34.6 1.0
SG F:CYS405 4.8 38.6 1.0
SG F:CYS362 4.8 33.1 1.0
NE2 F:GLN361 4.9 34.1 1.0
CG F:PRO203 4.9 39.7 1.0
C F:SER358 5.0 38.5 1.0
OG F:SER358 5.0 38.5 1.0

Iron binding site 8 out of 28 in 8q0a

Go back to Iron Binding Sites List in 8q0a
Iron binding site 8 out of 28 in the Inward-Facing, Closed 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, Closed 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:37.9
occ:1.00
 FE2 F:SF4502 0.0 37.9 1.0
SG F:CYS365 2.2 34.6 1.0
S3 F:SF4502 2.3 37.9 1.0
S1 F:SF4502 2.3 37.9 1.0
S4 F:SF4502 2.3 37.9 1.0
FE4 F:SF4502 2.7 37.9 1.0
FE3 F:SF4502 2.7 37.9 1.0
FE1 F:SF4502 2.7 37.9 1.0
CB F:CYS365 3.0 34.6 1.0
OG F:SER358 3.9 38.5 1.0
S2 F:SF4502 3.9 37.9 1.0
CA F:CYS365 4.3 34.6 1.0
N F:CYS359 4.4 37.7 1.0
SG F:CYS362 4.5 33.1 1.0
CB F:SER358 4.5 38.5 1.0
N F:GLY360 4.6 34.2 1.0
C F:CYS365 4.6 34.6 1.0
CD2 F:LEU407 4.6 41.7 1.0
CA F:SER358 4.7 38.5 1.0
SG F:CYS405 4.7 38.6 1.0
SG F:CYS359 4.8 37.7 1.0
N F:ARG366 4.8 32.1 1.0
CB F:LEU407 4.8 41.7 1.0
N F:GLY408 4.9 39.9 1.0
C F:SER358 5.0 38.5 1.0
N F:CYS365 5.0 34.6 1.0

Iron binding site 9 out of 28 in 8q0a

Go back to Iron Binding Sites List in 8q0a
Iron binding site 9 out of 28 in the Inward-Facing, Closed 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, Closed 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:37.9
occ:1.00
 FE3 F:SF4502 0.0 37.9 1.0
S1 F:SF4502 2.3 37.9 1.0
S4 F:SF4502 2.3 37.9 1.0
SG F:CYS405 2.3 38.6 1.0
S2 F:SF4502 2.3 37.9 1.0
FE2 F:SF4502 2.7 37.9 1.0
FE1 F:SF4502 2.7 37.9 1.0
FE4 F:SF4502 2.7 37.9 1.0
CB F:CYS405 3.3 38.6 1.0
S3 F:SF4502 3.9 37.9 1.0
N F:CYS405 3.9 38.6 1.0
CB F:LEU407 4.1 41.7 1.0
CA F:CYS405 4.1 38.6 1.0
CG F:PRO203 4.4 39.7 1.0
C F:CYS405 4.5 38.6 1.0
CD1 F:ILE185 4.6 43.1 1.0
O F:CYS405 4.6 38.6 1.0
N F:LEU407 4.7 41.7 1.0
N F:GLY408 4.7 39.9 1.0
CD F:PRO203 4.7 39.7 1.0
SG F:CYS365 4.8 34.6 1.0
SG F:CYS359 4.8 37.7 1.0
SG F:CYS362 4.9 33.1 1.0
CA F:LEU407 4.9 41.7 1.0

Iron binding site 10 out of 28 in 8q0a

Go back to Iron Binding Sites List in 8q0a
Iron binding site 10 out of 28 in the Inward-Facing, Closed 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, Closed 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:37.9
occ:1.00
 FE4 F:SF4502 0.0 37.9 1.0
S3 F:SF4502 2.3 37.9 1.0
S1 F:SF4502 2.3 37.9 1.0
SG F:CYS362 2.3 33.1 1.0
S2 F:SF4502 2.3 37.9 1.0
FE2 F:SF4502 2.7 37.9 1.0
FE1 F:SF4502 2.7 37.9 1.0
FE3 F:SF4502 2.7 37.9 1.0
CB F:CYS362 3.4 33.1 1.0
N F:CYS362 3.8 33.1 1.0
S4 F:SF4502 3.9 37.9 1.0
CA F:CYS362 4.1 33.1 1.0
N F:ILE404 4.2 34.5 1.0
CB F:ILE404 4.3 34.5 1.0
CB F:CYS365 4.3 34.6 1.0
O F:CYS362 4.5 33.1 1.0
C F:CYS362 4.5 33.1 1.0
SG F:CYS365 4.6 34.6 1.0
N F:CYS405 4.6 38.6 1.0
CB F:THR403 4.6 34.7 1.0
CG1 F:ILE404 4.7 34.5 1.0
SG F:CYS359 4.8 37.7 1.0
CA F:ILE404 4.8 34.5 1.0
CD1 F:ILE404 4.8 34.5 1.0
SG F:CYS405 4.8 38.6 1.0
C F:GLN361 4.9 34.1 1.0
N F:GLN361 4.9 34.1 1.0

Reference:

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
Page generated: Thu Aug 7 20:17:58 2025

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