Iron in PDB 8q0q: Outward-Facing, Slack Proteoliposome Complex I at 3.6 A. Initially Purified in Ddm

Enzymatic activity of Outward-Facing, Slack Proteoliposome Complex I at 3.6 A. Initially Purified in Ddm

All present enzymatic activity of Outward-Facing, Slack Proteoliposome Complex I at 3.6 A. Initially Purified in Ddm:
1.6.5.3; 1.6.99.3; 7.1.1.2;

Other elements in 8q0q:

The structure of Outward-Facing, Slack Proteoliposome Complex I at 3.6 A. Initially Purified in Ddm also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Potassium (K) 1 atom
Zinc (Zn) 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 Outward-Facing, Slack Proteoliposome Complex I at 3.6 A. Initially Purified in Ddm (pdb code 8q0q). 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, Slack Proteoliposome Complex I at 3.6 A. Initially Purified in Ddm, PDB code: 8q0q:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 28 in 8q0q

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Iron binding site 1 out of 28 in the Outward-Facing, Slack Proteoliposome Complex I at 3.6 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 Outward-Facing, Slack Proteoliposome Complex I at 3.6 A. Initially Purified in Ddm within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe202

b:66.7
occ:1.00
 FE1 B:SF4202 0.0 66.7 1.0
SG B:CYS119 2.2 35.7 1.0
S3 B:SF4202 2.3 66.7 1.0
S2 B:SF4202 2.3 66.7 1.0
S4 B:SF4202 2.3 66.7 1.0
FE4 B:SF4202 2.7 66.7 1.0
FE3 B:SF4202 2.7 66.7 1.0
FE2 B:SF4202 2.7 66.7 1.0
CB B:CYS119 3.1 35.7 1.0
N B:CYS119 3.8 35.7 1.0
SG B:CYS149 3.8 46.5 1.0
S1 B:SF4202 3.9 66.7 1.0
CA B:CYS119 4.0 35.7 1.0
OG1 B:THR91 4.2 39.9 1.0
SG B:CYS55 4.7 66.7 1.0
CE2 B:TYR126 4.8 66.7 1.0
SG B:CYS54 4.8 66.7 1.0
N B:SER118 4.8 37.3 1.0
C B:SER118 4.9 37.3 1.0
CQ2 D:2MR85 5.0 66.7 1.0

Iron binding site 2 out of 28 in 8q0q

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Iron binding site 2 out of 28 in the Outward-Facing, Slack Proteoliposome Complex I at 3.6 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 Outward-Facing, Slack Proteoliposome Complex I at 3.6 A. Initially Purified in Ddm within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe202

b:66.7
occ:1.00
 FE2 B:SF4202 0.0 66.7 1.0
S1 B:SF4202 2.3 66.7 1.0
SG B:CYS149 2.3 46.5 1.0
S3 B:SF4202 2.3 66.7 1.0
S4 B:SF4202 2.3 66.7 1.0
FE4 B:SF4202 2.7 66.7 1.0
FE1 B:SF4202 2.7 66.7 1.0
FE3 B:SF4202 2.7 66.7 1.0
CA B:CYS149 3.0 46.5 1.0
CB B:CYS149 3.1 46.5 1.0
C B:CYS149 3.5 46.5 1.0
SG B:CYS55 3.6 66.7 1.0
N B:PRO150 3.8 44.1 1.0
S2 B:SF4202 3.9 66.7 1.0
CA B:PRO150 4.0 44.1 1.0
O B:CYS149 4.2 46.5 1.0
O B:GLY148 4.3 54.2 1.0
N B:CYS149 4.4 46.5 1.0
CB B:PRO150 4.5 44.1 1.0
N B:SER118 4.6 37.3 1.0
CD B:PRO150 4.7 44.1 1.0
SG B:CYS119 4.7 35.7 1.0
C B:GLY148 4.8 54.2 1.0
SG B:CYS54 4.9 66.7 1.0
NE D:ARG105 4.9 66.7 1.0

Iron binding site 3 out of 28 in 8q0q

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Iron binding site 3 out of 28 in the Outward-Facing, Slack Proteoliposome Complex I at 3.6 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 Outward-Facing, Slack Proteoliposome Complex I at 3.6 A. Initially Purified in Ddm within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe202

b:66.7
occ:1.00
 FE3 B:SF4202 0.0 66.7 1.0
S1 B:SF4202 2.3 66.7 1.0
S2 B:SF4202 2.3 66.7 1.0
S4 B:SF4202 2.3 66.7 1.0
SG B:CYS54 2.3 66.7 1.0
FE4 B:SF4202 2.7 66.7 1.0
FE1 B:SF4202 2.7 66.7 1.0
FE2 B:SF4202 2.7 66.7 1.0
CB B:CYS54 3.3 66.7 1.0
S3 B:SF4202 3.9 66.7 1.0
CQ2 D:2MR85 4.0 66.7 1.0
N B:CYS54 4.1 66.7 1.0
CE1 D:HIS190 4.1 41.2 1.0
SG B:CYS149 4.1 46.5 1.0
CA B:CYS54 4.1 66.7 1.0
N B:CYS55 4.1 66.7 1.0
CG D:ARG105 4.4 66.7 1.0
SG B:CYS55 4.5 66.7 1.0
C B:CYS54 4.6 66.7 1.0
NE D:ARG105 4.7 66.7 1.0
SG B:CYS119 4.7 35.7 1.0
CD D:ARG105 4.8 66.7 1.0
ND1 D:HIS190 4.8 41.2 1.0
CB B:ALA53 4.9 40.6 1.0
NE2 D:HIS190 5.0 41.2 1.0

Iron binding site 4 out of 28 in 8q0q

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Iron binding site 4 out of 28 in the Outward-Facing, Slack Proteoliposome Complex I at 3.6 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 Outward-Facing, Slack Proteoliposome Complex I at 3.6 A. Initially Purified in Ddm within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe202

b:66.7
occ:1.00
 FE4 B:SF4202 0.0 66.7 1.0
S2 B:SF4202 2.3 66.7 1.0
SG B:CYS55 2.3 66.7 1.0
S1 B:SF4202 2.3 66.7 1.0
S3 B:SF4202 2.3 66.7 1.0
FE2 B:SF4202 2.7 66.7 1.0
FE3 B:SF4202 2.7 66.7 1.0
FE1 B:SF4202 2.7 66.7 1.0
CB B:CYS55 3.2 66.7 1.0
N B:CYS55 3.4 66.7 1.0
CA B:CYS55 3.8 66.7 1.0
S4 B:SF4202 3.8 66.7 1.0
CA B:GLY90 4.3 31.3 1.0
SG B:CYS54 4.5 66.7 1.0
C B:CYS54 4.5 66.7 1.0
N B:CYS54 4.6 66.7 1.0
SG B:CYS119 4.6 35.7 1.0
N B:GLY90 4.6 31.3 1.0
CA B:GLY117 4.6 42.9 1.0
CB B:CYS54 4.7 66.7 1.0
CB B:CYS119 4.7 35.7 1.0
CA B:CYS54 4.9 66.7 1.0
SG B:CYS149 4.9 46.5 1.0
C B:GLY90 4.9 31.3 1.0
N B:CYS119 4.9 35.7 1.0
N B:SER118 5.0 37.3 1.0
CB B:ALA53 5.0 40.6 1.0

Iron binding site 5 out of 28 in 8q0q

Go back to Iron Binding Sites List in 8q0q
Iron binding site 5 out of 28 in the Outward-Facing, Slack Proteoliposome Complex I at 3.6 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 Outward-Facing, Slack Proteoliposome Complex I at 3.6 A. Initially Purified in Ddm within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe301

b:73.2
occ:1.00
 FE1 E:FES301 0.0 73.2 1.0
S1 E:FES301 2.2 73.2 1.0
S2 E:FES301 2.2 73.2 1.0
SG E:CYS108 2.2 59.7 1.0
SG E:CYS103 2.2 56.9 1.0
FE2 E:FES301 2.7 73.2 1.0
CB E:CYS108 3.2 59.7 1.0
CB E:CYS103 3.3 56.9 1.0
CA E:CYS144 4.0 64.0 1.0
N E:LEU145 4.1 62.9 1.0
CA E:CYS148 4.2 71.7 1.0
N E:CYS108 4.2 59.7 1.0
CA E:CYS108 4.3 59.7 1.0
SG E:CYS144 4.5 64.0 1.0
CB E:THR105 4.5 58.9 1.0
OG1 E:THR105 4.5 58.9 1.0
N E:CYS148 4.5 71.7 1.0
CB E:CYS144 4.5 64.0 1.0
SG E:CYS148 4.5 71.7 1.0
CB E:CYS148 4.6 71.7 1.0
C E:CYS144 4.6 64.0 1.0
CA E:CYS103 4.7 56.9 1.0
C E:ALA147 4.7 67.8 1.0
O E:CYS103 4.8 56.9 1.0
O E:ALA147 4.8 67.8 1.0
C E:CYS103 4.9 56.9 1.0
N E:CYS144 4.9 64.0 1.0
N E:ALA147 5.0 67.8 1.0

Iron binding site 6 out of 28 in 8q0q

Go back to Iron Binding Sites List in 8q0q
Iron binding site 6 out of 28 in the Outward-Facing, Slack Proteoliposome Complex I at 3.6 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 Outward-Facing, Slack Proteoliposome Complex I at 3.6 A. Initially Purified in Ddm within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe301

b:73.2
occ:1.00
 FE2 E:FES301 0.0 73.2 1.0
S2 E:FES301 2.2 73.2 1.0
S1 E:FES301 2.2 73.2 1.0
SG E:CYS148 2.3 71.7 1.0
SG E:CYS144 2.3 64.0 1.0
FE1 E:FES301 2.7 73.2 1.0
CB E:CYS148 3.3 71.7 1.0
CB E:CYS144 3.3 64.0 1.0
CA E:CYS148 3.6 71.7 1.0
N E:CYS148 3.6 71.7 1.0
CA E:CYS144 3.6 64.0 1.0
N E:GLY146 3.8 65.2 1.0
N E:LEU145 3.8 62.9 1.0
N F:GLY103 3.9 68.8 1.0
N E:ALA147 4.0 67.8 1.0
C E:CYS144 4.1 64.0 1.0
CA E:GLY146 4.3 65.2 1.0
C E:ALA147 4.4 67.8 1.0
SG E:CYS103 4.4 56.9 1.0
SG E:CYS108 4.5 59.7 1.0
CA F:PRO102 4.6 60.4 1.0
C E:GLY146 4.6 65.2 1.0
CA F:GLY103 4.6 68.8 1.0
C F:PRO102 4.7 60.4 1.0
C E:LEU145 4.7 62.9 1.0
CA E:ALA147 4.8 67.8 1.0
N F:THR104 4.8 69.2 1.0
O F:GLU101 4.8 62.5 1.0
O F:THR104 4.9 69.2 1.0
CA E:LEU145 4.9 62.9 1.0
N E:CYS144 4.9 64.0 1.0

Iron binding site 7 out of 28 in 8q0q

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Iron binding site 7 out of 28 in the Outward-Facing, Slack Proteoliposome Complex I at 3.6 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 Outward-Facing, Slack Proteoliposome Complex I at 3.6 A. Initially Purified in Ddm within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe502

b:66.7
occ:1.00
 FE1 F:SF4502 0.0 66.7 1.0
SG F:CYS359 2.2 47.0 1.0
S3 F:SF4502 2.3 66.7 1.0
S2 F:SF4502 2.3 66.7 1.0
S4 F:SF4502 2.3 66.7 1.0
FE2 F:SF4502 2.7 66.7 1.0
FE3 F:SF4502 2.7 66.7 1.0
FE4 F:SF4502 2.7 66.7 1.0
CB F:CYS359 3.2 47.0 1.0
N F:GLY360 3.4 41.8 1.0
N F:CYS359 3.7 47.0 1.0
CA F:CYS359 3.8 47.0 1.0
N F:GLN361 3.8 44.8 1.0
S1 F:SF4502 3.9 66.7 1.0
C F:CYS359 4.0 47.0 1.0
CG F:GLN361 4.2 44.8 1.0
OG F:SER358 4.3 44.4 1.0
CA F:GLY360 4.3 41.8 1.0
N F:CYS362 4.4 38.7 1.0
CD F:PRO203 4.4 50.6 1.0
C F:GLY360 4.5 41.8 1.0
SG F:CYS362 4.7 38.7 1.0
SG F:CYS365 4.7 41.1 1.0
CA F:GLN361 4.8 44.8 1.0
SG F:CYS405 4.8 47.2 1.0
C F:SER358 4.8 44.4 1.0
CB F:GLN361 4.8 44.8 1.0
CG F:PRO203 4.8 50.6 1.0

Iron binding site 8 out of 28 in 8q0q

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Iron binding site 8 out of 28 in the Outward-Facing, Slack Proteoliposome Complex I at 3.6 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 Outward-Facing, Slack Proteoliposome Complex I at 3.6 A. Initially Purified in Ddm within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe502

b:66.7
occ:1.00
 FE2 F:SF4502 0.0 66.7 1.0
SG F:CYS365 2.2 41.1 1.0
S3 F:SF4502 2.3 66.7 1.0
S1 F:SF4502 2.3 66.7 1.0
S4 F:SF4502 2.3 66.7 1.0
FE4 F:SF4502 2.7 66.7 1.0
FE1 F:SF4502 2.7 66.7 1.0
FE3 F:SF4502 2.7 66.7 1.0
OG F:SER358 2.9 44.4 1.0
CB F:CYS365 3.0 41.1 1.0
S2 F:SF4502 3.9 66.7 1.0
CB F:SER358 4.0 44.4 1.0
CA F:CYS365 4.3 41.1 1.0
N F:GLY360 4.3 41.8 1.0
N F:CYS359 4.3 47.0 1.0
SG F:CYS362 4.5 38.7 1.0
C F:CYS365 4.5 41.1 1.0
CA F:SER358 4.5 44.4 1.0
N F:ARG366 4.7 40.6 1.0
O F:CYS362 4.7 38.7 1.0
SG F:CYS359 4.7 47.0 1.0
SG F:CYS405 4.8 47.2 1.0
C F:SER358 4.8 44.4 1.0
N F:GLY408 4.9 47.8 1.0
CD2 F:LEU407 4.9 50.1 1.0
CA F:GLY360 4.9 41.8 1.0
N F:CYS365 4.9 41.1 1.0

Iron binding site 9 out of 28 in 8q0q

Go back to Iron Binding Sites List in 8q0q
Iron binding site 9 out of 28 in the Outward-Facing, Slack Proteoliposome Complex I at 3.6 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 Outward-Facing, Slack Proteoliposome Complex I at 3.6 A. Initially Purified in Ddm within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe502

b:66.7
occ:1.00
 FE3 F:SF4502 0.0 66.7 1.0
SG F:CYS405 2.3 47.2 1.0
S1 F:SF4502 2.3 66.7 1.0
S2 F:SF4502 2.3 66.7 1.0
S4 F:SF4502 2.3 66.7 1.0
FE1 F:SF4502 2.7 66.7 1.0
FE2 F:SF4502 2.7 66.7 1.0
FE4 F:SF4502 2.7 66.7 1.0
CB F:CYS405 3.3 47.2 1.0
S3 F:SF4502 3.9 66.7 1.0
N F:CYS405 3.9 47.2 1.0
O F:CYS405 4.0 47.2 1.0
CA F:CYS405 4.0 47.2 1.0
CB F:LEU407 4.1 50.1 1.0
C F:CYS405 4.2 47.2 1.0
CG F:PRO203 4.5 50.6 1.0
N F:GLY408 4.6 47.8 1.0
CD1 F:ILE185 4.6 47.7 1.0
SG F:CYS359 4.7 47.0 1.0
SG F:CYS365 4.7 41.1 1.0
N F:LEU407 4.7 50.1 1.0
SG F:CYS362 4.9 38.7 1.0
CA F:LEU407 4.9 50.1 1.0
CD F:PRO203 5.0 50.6 1.0
CD1 F:LEU407 5.0 50.1 1.0

Iron binding site 10 out of 28 in 8q0q

Go back to Iron Binding Sites List in 8q0q
Iron binding site 10 out of 28 in the Outward-Facing, Slack Proteoliposome Complex I at 3.6 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 Outward-Facing, Slack Proteoliposome Complex I at 3.6 A. Initially Purified in Ddm within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe502

b:66.7
occ:1.00
 FE4 F:SF4502 0.0 66.7 1.0
SG F:CYS362 2.3 38.7 1.0
S3 F:SF4502 2.3 66.7 1.0
S1 F:SF4502 2.3 66.7 1.0
S2 F:SF4502 2.3 66.7 1.0
FE2 F:SF4502 2.7 66.7 1.0
FE1 F:SF4502 2.7 66.7 1.0
FE3 F:SF4502 2.7 66.7 1.0
CB F:CYS362 3.2 38.7 1.0
S4 F:SF4502 3.9 66.7 1.0
O F:CYS362 3.9 38.7 1.0
N F:CYS362 3.9 38.7 1.0
N F:ILE404 4.0 42.8 1.0
CA F:CYS362 4.0 38.7 1.0
CB F:THR403 4.2 39.2 1.0
CB F:CYS365 4.3 41.1 1.0
CB F:ILE404 4.3 42.8 1.0
C F:CYS362 4.4 38.7 1.0
N F:CYS405 4.4 47.2 1.0
SG F:CYS365 4.5 41.1 1.0
CG1 F:ILE404 4.6 42.8 1.0
CA F:ILE404 4.7 42.8 1.0
SG F:CYS359 4.7 47.0 1.0
CG2 F:THR403 4.7 39.2 1.0
SG F:CYS405 4.8 47.2 1.0
CA F:THR403 4.8 39.2 1.0
CG F:GLN361 4.8 44.8 1.0
CD1 F:ILE404 4.8 42.8 1.0
C F:THR403 4.9 39.2 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 13:32:01 2024

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