Iron in PDB 8q48: Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng.

Enzymatic activity of Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng.

All present enzymatic activity of Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng.:
1.6.5.3; 1.6.99.3; 7.1.1.2;

Other elements in 8q48:

The structure of Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng. also contains other interesting chemical elements:

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

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 Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng. (pdb code 8q48). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 28 binding sites of Iron where determined in the Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng., PDB code: 8q48:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 28 in 8q48

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Iron binding site 1 out of 28 in the Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe201

b:29.7
occ:1.00
 FE1 B:SF4201 0.0 29.7 1.0
SG B:CYS119 2.2 24.5 1.0
S3 B:SF4201 2.3 29.7 1.0
S2 B:SF4201 2.3 29.7 1.0
S4 B:SF4201 2.3 29.7 1.0
FE3 B:SF4201 2.7 29.7 1.0
FE4 B:SF4201 2.7 29.7 1.0
FE2 B:SF4201 2.7 29.7 1.0
CB B:CYS119 3.2 24.5 1.0
O B:HOH328 3.5 26.2 1.0
S1 B:SF4201 3.9 29.7 1.0
OG1 B:THR91 3.9 26.4 1.0
N B:CYS119 4.0 24.5 1.0
CA B:CYS119 4.2 24.5 1.0
O B:HOH311 4.4 28.0 1.0
SG B:CYS149 4.4 24.5 1.0
CQ2 D:2MR85 4.5 25.9 1.0
CE1 B:TYR126 4.8 24.2 1.0
SG B:CYS54 4.8 26.5 1.0
SG B:CYS55 4.8 26.9 1.0
N B:THR91 4.9 26.4 1.0
C B:GLY90 5.0 26.3 1.0
NH2 D:2MR85 5.0 25.9 1.0

Iron binding site 2 out of 28 in 8q48

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Iron binding site 2 out of 28 in the Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe201

b:29.7
occ:1.00
 FE2 B:SF4201 0.0 29.7 1.0
SG B:CYS149 2.2 24.5 1.0
S1 B:SF4201 2.3 29.7 1.0
S3 B:SF4201 2.3 29.7 1.0
S4 B:SF4201 2.3 29.7 1.0
FE4 B:SF4201 2.7 29.7 1.0
FE3 B:SF4201 2.7 29.7 1.0
FE1 B:SF4201 2.7 29.7 1.0
CB B:CYS149 3.4 24.5 1.0
CA B:CYS149 3.4 24.5 1.0
C B:CYS149 3.7 24.5 1.0
O B:HOH328 3.9 26.2 1.0
S2 B:SF4201 3.9 29.7 1.0
N B:PRO150 4.1 25.4 1.0
O B:CYS149 4.1 24.5 1.0
NE D:ARG105 4.1 24.7 1.0
CD2 D:HIS190 4.4 25.5 1.0
CA B:PRO150 4.5 25.4 1.0
NE2 D:HIS190 4.5 25.5 1.0
SG B:CYS55 4.6 26.9 1.0
NH2 D:ARG105 4.7 24.7 1.0
SG B:CYS119 4.7 24.5 1.0
N B:CYS149 4.8 24.5 1.0
CD B:PRO150 4.8 25.4 1.0
SG B:CYS54 4.8 26.5 1.0
CZ D:ARG105 4.9 24.7 1.0
O B:GLY148 4.9 24.6 1.0
CD D:ARG105 4.9 24.7 1.0

Iron binding site 3 out of 28 in 8q48

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Iron binding site 3 out of 28 in the Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe201

b:29.7
occ:1.00
 FE3 B:SF4201 0.0 29.7 1.0
SG B:CYS54 2.3 26.5 1.0
S1 B:SF4201 2.3 29.7 1.0
S4 B:SF4201 2.3 29.7 1.0
S2 B:SF4201 2.3 29.7 1.0
FE4 B:SF4201 2.7 29.7 1.0
FE1 B:SF4201 2.7 29.7 1.0
FE2 B:SF4201 2.7 29.7 1.0
CB B:CYS54 3.2 26.5 1.0
CQ2 D:2MR85 3.7 25.9 1.0
S3 B:SF4201 3.9 29.7 1.0
NE2 D:HIS190 3.9 25.5 1.0
N B:CYS54 4.0 26.5 1.0
CA B:CYS54 4.1 26.5 1.0
N B:CYS55 4.3 26.9 1.0
CG D:ARG105 4.3 24.7 1.0
C B:CYS54 4.5 26.5 1.0
CD2 D:HIS190 4.6 25.5 1.0
NE D:ARG105 4.7 24.7 1.0
CD D:ARG105 4.8 24.7 1.0
SG B:CYS119 4.8 24.5 1.0
SG B:CYS149 4.8 24.5 1.0
CB B:ALA53 4.8 27.6 1.0
NH2 D:2MR85 4.8 25.9 1.0
SG B:CYS55 4.8 26.9 1.0
CE1 D:HIS190 4.9 25.5 1.0
CB D:ARG105 4.9 24.7 1.0

Iron binding site 4 out of 28 in 8q48

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Iron binding site 4 out of 28 in the Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe201

b:29.7
occ:1.00
 FE4 B:SF4201 0.0 29.7 1.0
S3 B:SF4201 2.3 29.7 1.0
SG B:CYS55 2.3 26.9 1.0
S2 B:SF4201 2.3 29.7 1.0
S1 B:SF4201 2.3 29.7 1.0
FE2 B:SF4201 2.7 29.7 1.0
FE3 B:SF4201 2.7 29.7 1.0
FE1 B:SF4201 2.7 29.7 1.0
CB B:CYS55 3.3 26.9 1.0
N B:CYS55 3.6 26.9 1.0
O B:HOH311 3.7 28.0 1.0
CA B:CYS55 3.9 26.9 1.0
S4 B:SF4201 3.9 29.7 1.0
CB B:PRO150 4.5 25.4 1.0
CA B:PRO150 4.5 25.4 1.0
C B:CYS54 4.6 26.5 1.0
CA B:GLY90 4.6 26.3 1.0
SG B:CYS54 4.6 26.5 1.0
CA B:GLY117 4.7 25.1 1.0
CB B:CYS54 4.7 26.5 1.0
SG B:CYS119 4.8 24.5 1.0
SG B:CYS149 4.8 24.5 1.0
CA B:CYS149 4.9 24.5 1.0
N B:PRO150 4.9 25.4 1.0
N B:CYS54 5.0 26.5 1.0

Iron binding site 5 out of 28 in 8q48

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Iron binding site 5 out of 28 in the Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng. within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe301

b:49.0
occ:1.00
 FE1 E:FES301 0.0 49.0 1.0
S2 E:FES301 2.2 49.0 1.0
S1 E:FES301 2.2 49.0 1.0
SG E:CYS108 2.3 46.7 1.0
SG E:CYS103 2.3 47.8 1.0
FE2 E:FES301 2.7 49.0 1.0
CB E:CYS108 3.3 46.7 1.0
CB E:CYS103 3.3 47.8 1.0
CA E:CYS144 4.1 45.0 1.0
N E:CYS108 4.2 46.7 1.0
N E:LEU145 4.3 47.0 1.0
CA E:CYS108 4.3 46.7 1.0
SG E:CYS144 4.5 45.0 1.0
CB E:CYS144 4.6 45.0 1.0
CA E:CYS103 4.7 47.8 1.0
SG E:CYS148 4.7 48.4 1.0
CA E:CYS148 4.7 48.4 1.0
C E:CYS144 4.8 45.0 1.0
CG E:MET153 4.8 50.5 1.0
C E:CYS103 4.9 47.8 1.0
CB E:THR105 4.9 44.1 1.0
N E:CYS144 4.9 45.0 1.0
CB E:CYS148 4.9 48.4 1.0
SD E:MET153 4.9 50.5 1.0
N E:THR105 5.0 44.1 1.0
O E:THR105 5.0 44.1 1.0

Iron binding site 6 out of 28 in 8q48

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Iron binding site 6 out of 28 in the Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng. within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe301

b:49.0
occ:1.00
 FE2 E:FES301 0.0 49.0 1.0
S2 E:FES301 2.2 49.0 1.0
S1 E:FES301 2.2 49.0 1.0
SG E:CYS148 2.3 48.4 1.0
SG E:CYS144 2.3 45.0 1.0
FE1 E:FES301 2.7 49.0 1.0
CB E:CYS144 3.3 45.0 1.0
CB E:CYS148 3.3 48.4 1.0
CA E:CYS144 3.6 45.0 1.0
CA E:CYS148 3.7 48.4 1.0
N E:CYS148 3.8 48.4 1.0
N E:LEU145 4.0 47.0 1.0
N E:GLY146 4.1 47.5 1.0
C E:CYS144 4.2 45.0 1.0
N E:ALA147 4.3 49.4 1.0
N F:GLY103 4.3 45.4 1.0
SG E:CYS103 4.4 47.8 1.0
SG E:CYS108 4.5 46.7 1.0
C E:ALA147 4.5 49.4 1.0
CA E:GLY146 4.7 47.5 1.0
CB E:PRO107 4.8 45.3 1.0
CG E:PRO107 4.9 45.3 1.0
CA F:PRO102 4.9 42.8 1.0
C E:GLY146 4.9 47.5 1.0
N E:CYS144 4.9 45.0 1.0
C E:LEU145 5.0 47.0 1.0

Iron binding site 7 out of 28 in 8q48

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Iron binding site 7 out of 28 in the Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng. within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe502

b:36.7
occ:1.00
 FE1 F:SF4502 0.0 36.7 1.0
SG F:CYS359 2.3 34.5 1.0
S3 F:SF4502 2.3 36.7 1.0
S4 F:SF4502 2.3 36.7 1.0
S2 F:SF4502 2.3 36.7 1.0
FE3 F:SF4502 2.7 36.7 1.0
FE4 F:SF4502 2.7 36.7 1.0
FE2 F:SF4502 2.7 36.7 1.0
CB F:CYS359 3.3 34.5 1.0
N F:GLN361 3.8 32.6 1.0
N F:CYS359 3.8 34.5 1.0
N F:GLY360 3.8 33.0 1.0
S1 F:SF4502 3.9 36.7 1.0
CA F:CYS359 3.9 34.5 1.0
CB F:GLN361 4.0 32.6 1.0
C F:CYS359 4.1 34.5 1.0
CD F:PRO203 4.3 35.7 1.0
CA F:GLN361 4.4 32.6 1.0
N F:CYS362 4.5 31.1 1.0
OG F:SER358 4.7 35.1 1.0
C F:GLY360 4.7 33.0 1.0
CA F:GLY360 4.8 33.0 1.0
NE2 F:GLN361 4.8 32.6 1.0
SG F:CYS365 4.8 32.3 1.0
SG F:CYS405 4.8 34.3 1.0
C F:SER358 4.8 35.1 1.0
CG F:PRO203 4.8 35.7 1.0
SG F:CYS362 4.9 31.1 1.0

Iron binding site 8 out of 28 in 8q48

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Iron binding site 8 out of 28 in the Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng. within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe502

b:36.7
occ:1.00
 FE2 F:SF4502 0.0 36.7 1.0
SG F:CYS365 2.2 32.3 1.0
S1 F:SF4502 2.3 36.7 1.0
S3 F:SF4502 2.3 36.7 1.0
S4 F:SF4502 2.3 36.7 1.0
FE4 F:SF4502 2.7 36.7 1.0
FE3 F:SF4502 2.7 36.7 1.0
FE1 F:SF4502 2.7 36.7 1.0
CB F:CYS365 3.0 32.3 1.0
OG F:SER358 3.3 35.1 1.0
S2 F:SF4502 3.9 36.7 1.0
CB F:SER358 4.3 35.1 1.0
CA F:CYS365 4.3 32.3 1.0
N F:CYS359 4.3 34.5 1.0
CD2 F:LEU407 4.4 37.0 1.0
CA F:SER358 4.4 35.1 1.0
SG F:CYS362 4.4 31.1 1.0
C F:CYS365 4.5 32.3 1.0
N F:GLY360 4.7 33.0 1.0
CB F:LEU407 4.7 37.0 1.0
SG F:CYS405 4.8 34.3 1.0
C F:SER358 4.8 35.1 1.0
N F:GLY408 4.8 35.6 1.0
SG F:CYS359 4.8 34.5 1.0
N F:ARG366 4.9 31.3 1.0
O F:CYS365 4.9 32.3 1.0
CG F:LEU407 5.0 37.0 1.0
N F:CYS365 5.0 32.3 1.0

Iron binding site 9 out of 28 in 8q48

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Iron binding site 9 out of 28 in the Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng. within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe502

b:36.7
occ:1.00
 FE3 F:SF4502 0.0 36.7 1.0
S1 F:SF4502 2.3 36.7 1.0
S2 F:SF4502 2.3 36.7 1.0
SG F:CYS405 2.3 34.3 1.0
S4 F:SF4502 2.3 36.7 1.0
FE1 F:SF4502 2.7 36.7 1.0
FE2 F:SF4502 2.7 36.7 1.0
FE4 F:SF4502 2.7 36.7 1.0
CB F:CYS405 3.3 34.3 1.0
S3 F:SF4502 3.9 36.7 1.0
N F:CYS405 4.0 34.3 1.0
CA F:CYS405 4.1 34.3 1.0
CB F:LEU407 4.1 37.0 1.0
CG F:PRO203 4.3 35.7 1.0
C F:CYS405 4.3 34.3 1.0
O F:CYS405 4.4 34.3 1.0
CD1 F:ILE185 4.4 38.3 1.0
N F:LEU407 4.6 37.0 1.0
N F:GLY408 4.7 35.6 1.0
CD F:PRO203 4.7 35.7 1.0
SG F:CYS359 4.8 34.5 1.0
SG F:CYS365 4.8 32.3 1.0
SG F:CYS362 4.8 31.1 1.0
CA F:LEU407 4.9 37.0 1.0

Iron binding site 10 out of 28 in 8q48

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Iron binding site 10 out of 28 in the Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng. within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe502

b:36.7
occ:1.00
 FE4 F:SF4502 0.0 36.7 1.0
S3 F:SF4502 2.3 36.7 1.0
SG F:CYS362 2.3 31.1 1.0
S1 F:SF4502 2.3 36.7 1.0
S2 F:SF4502 2.3 36.7 1.0
FE2 F:SF4502 2.7 36.7 1.0
FE1 F:SF4502 2.7 36.7 1.0
FE3 F:SF4502 2.7 36.7 1.0
CB F:CYS362 3.4 31.1 1.0
N F:CYS362 3.6 31.1 1.0
S4 F:SF4502 3.9 36.7 1.0
CA F:CYS362 4.0 31.1 1.0
N F:ILE404 4.2 31.9 1.0
CB F:CYS365 4.4 32.3 1.0
O F:CYS362 4.4 31.1 1.0
CB F:THR403 4.4 31.4 1.0
CB F:ILE404 4.4 31.9 1.0
C F:CYS362 4.6 31.1 1.0
SG F:CYS365 4.6 32.3 1.0
N F:CYS405 4.6 34.3 1.0
CG1 F:ILE404 4.7 31.9 1.0
SG F:CYS359 4.8 34.5 1.0
CD1 F:ILE404 4.8 31.9 1.0
CG2 F:THR403 4.8 31.4 1.0
C F:GLN361 4.8 32.6 1.0
CB F:GLN361 4.8 32.6 1.0
N F:GLN361 4.8 32.6 1.0
SG F:CYS405 4.8 34.3 1.0
CA F:ILE404 4.9 31.9 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: Sat Aug 10 14:26:13 2024

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