Iron in PDB 8q49: Outward-Facing, OPEN2 Proteoliposome Complex I at 2.6 A. Initially Purified in Lmng.

Enzymatic activity of Outward-Facing, OPEN2 Proteoliposome Complex I at 2.6 A. Initially Purified in Lmng.

All present enzymatic activity of Outward-Facing, OPEN2 Proteoliposome Complex I at 2.6 A. Initially Purified in Lmng.:
1.6.5.3; 1.6.99.3; 7.1.1.2;

Other elements in 8q49:

The structure of Outward-Facing, OPEN2 Proteoliposome Complex I at 2.6 A. Initially Purified in Lmng. also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Zinc (Zn) 2 atoms
Potassium (K) 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, OPEN2 Proteoliposome Complex I at 2.6 A. Initially Purified in Lmng. (pdb code 8q49). 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, OPEN2 Proteoliposome Complex I at 2.6 A. Initially Purified in Lmng., PDB code: 8q49:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 28 in 8q49

Go back to Iron Binding Sites List in 8q49
Iron binding site 1 out of 28 in the Outward-Facing, OPEN2 Proteoliposome Complex I at 2.6 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, OPEN2 Proteoliposome Complex I at 2.6 A. Initially Purified in Lmng. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe201

b:37.6
occ:1.00
 FE1 B:SF4201 0.0 37.6 1.0
SG B:CYS119 2.3 30.7 1.0
S3 B:SF4201 2.3 37.6 1.0
S4 B:SF4201 2.3 37.6 1.0
S2 B:SF4201 2.3 37.6 1.0
FE4 B:SF4201 2.7 37.6 1.0
FE3 B:SF4201 2.7 37.6 1.0
FE2 B:SF4201 2.7 37.6 1.0
CB B:CYS119 3.2 30.7 1.0
O B:HOH312 3.7 30.8 1.0
S1 B:SF4201 3.9 37.6 1.0
N B:CYS119 4.0 30.7 1.0
OG1 B:THR91 4.1 31.5 1.0
CA B:CYS119 4.2 30.7 1.0
SG B:CYS149 4.4 32.9 1.0
O B:HOH303 4.5 33.6 1.0
CQ2 D:2MR85 4.6 38.0 1.0
N B:THR91 4.9 31.5 1.0
SG B:CYS54 4.9 33.0 1.0
CE1 B:TYR126 4.9 27.3 1.0
SG B:CYS55 4.9 33.5 1.0

Iron binding site 2 out of 28 in 8q49

Go back to Iron Binding Sites List in 8q49
Iron binding site 2 out of 28 in the Outward-Facing, OPEN2 Proteoliposome Complex I at 2.6 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, OPEN2 Proteoliposome Complex I at 2.6 A. Initially Purified in Lmng. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe201

b:37.6
occ:1.00
 FE2 B:SF4201 0.0 37.6 1.0
SG B:CYS149 2.3 32.9 1.0
S1 B:SF4201 2.3 37.6 1.0
S3 B:SF4201 2.3 37.6 1.0
S4 B:SF4201 2.3 37.6 1.0
FE4 B:SF4201 2.7 37.6 1.0
FE1 B:SF4201 2.7 37.6 1.0
FE3 B:SF4201 2.7 37.6 1.0
CB B:CYS149 3.4 32.9 1.0
CA B:CYS149 3.4 32.9 1.0
C B:CYS149 3.7 32.9 1.0
S2 B:SF4201 3.9 37.6 1.0
N B:PRO150 4.1 33.2 1.0
O B:HOH312 4.1 30.8 1.0
NE D:ARG105 4.2 36.1 1.0
O B:CYS149 4.2 32.9 1.0
CD2 D:HIS190 4.4 36.6 1.0
CA B:PRO150 4.5 33.2 1.0
NE2 D:HIS190 4.5 36.6 1.0
SG B:CYS55 4.5 33.5 1.0
O B:GLY148 4.7 31.9 1.0
SG B:CYS119 4.7 30.7 1.0
N B:CYS149 4.7 32.9 1.0
CD B:PRO150 4.8 33.2 1.0
SG B:CYS54 4.8 33.0 1.0
NH2 D:ARG105 4.8 36.1 1.0
CB B:PRO150 5.0 33.2 1.0
CD D:ARG105 5.0 36.1 1.0

Iron binding site 3 out of 28 in 8q49

Go back to Iron Binding Sites List in 8q49
Iron binding site 3 out of 28 in the Outward-Facing, OPEN2 Proteoliposome Complex I at 2.6 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, OPEN2 Proteoliposome Complex I at 2.6 A. Initially Purified in Lmng. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe201

b:37.6
occ:1.00
 FE3 B:SF4201 0.0 37.6 1.0
SG B:CYS54 2.3 33.0 1.0
S1 B:SF4201 2.3 37.6 1.0
S4 B:SF4201 2.3 37.6 1.0
S2 B:SF4201 2.3 37.6 1.0
FE4 B:SF4201 2.7 37.6 1.0
FE1 B:SF4201 2.7 37.6 1.0
FE2 B:SF4201 2.7 37.6 1.0
CB B:CYS54 3.3 33.0 1.0
CQ2 D:2MR85 3.7 38.0 1.0
N B:CYS54 3.9 33.0 1.0
S3 B:SF4201 3.9 37.6 1.0
NE2 D:HIS190 3.9 36.6 1.0
CA B:CYS54 4.1 33.0 1.0
N B:CYS55 4.2 33.5 1.0
CG D:ARG105 4.3 36.1 1.0
C B:CYS54 4.5 33.0 1.0
CB B:ALA53 4.6 32.9 1.0
CD2 D:HIS190 4.7 36.6 1.0
SG B:CYS149 4.7 32.9 1.0
SG B:CYS119 4.8 30.7 1.0
CD D:ARG105 4.8 36.1 1.0
SG B:CYS55 4.8 33.5 1.0
NE D:ARG105 4.8 36.1 1.0
NH2 D:2MR85 4.9 38.0 1.0
C B:ALA53 4.9 32.9 1.0
CE1 D:HIS190 4.9 36.6 1.0
CB D:ARG105 5.0 36.1 1.0

Iron binding site 4 out of 28 in 8q49

Go back to Iron Binding Sites List in 8q49
Iron binding site 4 out of 28 in the Outward-Facing, OPEN2 Proteoliposome Complex I at 2.6 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, OPEN2 Proteoliposome Complex I at 2.6 A. Initially Purified in Lmng. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe201

b:37.6
occ:1.00
 FE4 B:SF4201 0.0 37.6 1.0
SG B:CYS55 2.3 33.5 1.0
S3 B:SF4201 2.3 37.6 1.0
S2 B:SF4201 2.3 37.6 1.0
S1 B:SF4201 2.3 37.6 1.0
FE2 B:SF4201 2.7 37.6 1.0
FE3 B:SF4201 2.7 37.6 1.0
FE1 B:SF4201 2.7 37.6 1.0
CB B:CYS55 3.3 33.5 1.0
N B:CYS55 3.6 33.5 1.0
O B:HOH303 3.8 33.6 1.0
S4 B:SF4201 3.9 37.6 1.0
CA B:CYS55 3.9 33.5 1.0
CB B:PRO150 4.6 33.2 1.0
CA B:PRO150 4.6 33.2 1.0
C B:CYS54 4.6 33.0 1.0
CA B:GLY117 4.6 31.7 1.0
SG B:CYS54 4.6 33.0 1.0
CB B:CYS54 4.8 33.0 1.0
SG B:CYS119 4.8 30.7 1.0
CA B:GLY90 4.8 32.7 1.0
SG B:CYS149 4.9 32.9 1.0
N B:CYS54 4.9 33.0 1.0
CA B:CYS149 5.0 32.9 1.0
CB B:CYS119 5.0 30.7 1.0
CA B:CYS54 5.0 33.0 1.0

Iron binding site 5 out of 28 in 8q49

Go back to Iron Binding Sites List in 8q49
Iron binding site 5 out of 28 in the Outward-Facing, OPEN2 Proteoliposome Complex I at 2.6 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, OPEN2 Proteoliposome Complex I at 2.6 A. Initially Purified in Lmng. within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe301

b:48.0
occ:1.00
 FE1 E:FES301 0.0 48.0 1.0
S2 E:FES301 2.2 48.0 1.0
S1 E:FES301 2.2 48.0 1.0
SG E:CYS103 2.3 48.0 1.0
SG E:CYS108 2.3 47.4 1.0
FE2 E:FES301 2.7 48.0 1.0
CB E:CYS103 3.3 48.0 1.0
CB E:CYS108 3.3 47.4 1.0
CA E:CYS144 4.1 47.0 1.0
N E:CYS108 4.2 47.4 1.0
CA E:CYS108 4.3 47.4 1.0
N E:LEU145 4.4 48.0 1.0
SG E:CYS144 4.4 47.0 1.0
CB E:CYS144 4.5 47.0 1.0
CA E:CYS148 4.6 50.2 1.0
CA E:CYS103 4.6 48.0 1.0
OG1 E:THR105 4.7 46.9 1.0
SG E:CYS148 4.7 50.2 1.0
CB E:THR105 4.8 46.9 1.0
C E:CYS144 4.8 47.0 1.0
CG E:MET153 4.9 51.1 1.0
C E:CYS103 4.9 48.0 1.0
N E:CYS148 5.0 50.2 1.0
N E:CYS144 5.0 47.0 1.0
N E:THR105 5.0 46.9 1.0

Iron binding site 6 out of 28 in 8q49

Go back to Iron Binding Sites List in 8q49
Iron binding site 6 out of 28 in the Outward-Facing, OPEN2 Proteoliposome Complex I at 2.6 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, OPEN2 Proteoliposome Complex I at 2.6 A. Initially Purified in Lmng. within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe301

b:48.0
occ:1.00
 FE2 E:FES301 0.0 48.0 1.0
S1 E:FES301 2.2 48.0 1.0
S2 E:FES301 2.2 48.0 1.0
SG E:CYS148 2.3 50.2 1.0
SG E:CYS144 2.3 47.0 1.0
FE1 E:FES301 2.7 48.0 1.0
CB E:CYS144 3.3 47.0 1.0
CB E:CYS148 3.3 50.2 1.0
CA E:CYS148 3.6 50.2 1.0
N E:CYS148 3.7 50.2 1.0
CA E:CYS144 3.7 47.0 1.0
N E:LEU145 4.1 48.0 1.0
N E:GLY146 4.2 47.6 1.0
N F:GLY103 4.2 51.3 1.0
C E:CYS144 4.3 47.0 1.0
N E:ALA147 4.3 50.0 1.0
SG E:CYS103 4.4 48.0 1.0
C E:ALA147 4.4 50.0 1.0
SG E:CYS108 4.6 47.4 1.0
CA F:PRO102 4.7 47.7 1.0
CB E:PRO107 4.8 46.6 1.0
CA E:GLY146 4.8 47.6 1.0
CG E:PRO107 4.8 46.6 1.0
C E:GLY146 4.9 47.6 1.0

Iron binding site 7 out of 28 in 8q49

Go back to Iron Binding Sites List in 8q49
Iron binding site 7 out of 28 in the Outward-Facing, OPEN2 Proteoliposome Complex I at 2.6 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, OPEN2 Proteoliposome Complex I at 2.6 A. Initially Purified in Lmng. within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe501

b:40.8
occ:1.00
 FE1 F:SF4501 0.0 40.8 1.0
SG F:CYS359 2.3 39.3 1.0
S3 F:SF4501 2.3 40.8 1.0
S2 F:SF4501 2.3 40.8 1.0
S4 F:SF4501 2.3 40.8 1.0
FE4 F:SF4501 2.7 40.8 1.0
FE2 F:SF4501 2.7 40.8 1.0
FE3 F:SF4501 2.7 40.8 1.0
CB F:CYS359 3.3 39.3 1.0
N F:CYS359 3.8 39.3 1.0
S1 F:SF4501 3.9 40.8 1.0
CA F:CYS359 3.9 39.3 1.0
N F:GLN361 3.9 37.4 1.0
N F:GLY360 4.0 37.4 1.0
CB F:GLN361 4.1 37.4 1.0
CD F:PRO203 4.2 41.2 1.0
C F:CYS359 4.2 39.3 1.0
N F:CYS362 4.5 38.7 1.0
CA F:GLN361 4.6 37.4 1.0
OE1 F:GLN361 4.7 37.4 1.0
SG F:CYS362 4.7 38.7 1.0
CG F:PRO203 4.8 41.2 1.0
SG F:CYS365 4.8 38.4 1.0
SG F:CYS405 4.8 40.4 1.0
CD1 F:ILE185 4.9 44.2 1.0
OG F:SER358 4.9 40.6 1.0
C F:SER358 4.9 40.6 1.0
CG1 F:ILE185 4.9 44.2 1.0
C F:GLY360 4.9 37.4 1.0

Iron binding site 8 out of 28 in 8q49

Go back to Iron Binding Sites List in 8q49
Iron binding site 8 out of 28 in the Outward-Facing, OPEN2 Proteoliposome Complex I at 2.6 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, OPEN2 Proteoliposome Complex I at 2.6 A. Initially Purified in Lmng. within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe501

b:40.8
occ:1.00
 FE2 F:SF4501 0.0 40.8 1.0
SG F:CYS365 2.2 38.4 1.0
S3 F:SF4501 2.3 40.8 1.0
S1 F:SF4501 2.3 40.8 1.0
S4 F:SF4501 2.3 40.8 1.0
FE4 F:SF4501 2.7 40.8 1.0
FE1 F:SF4501 2.7 40.8 1.0
FE3 F:SF4501 2.7 40.8 1.0
CB F:CYS365 3.1 38.4 1.0
OG F:SER358 3.5 40.6 1.0
S2 F:SF4501 3.9 40.8 1.0
N F:CYS359 4.3 39.3 1.0
CA F:CYS365 4.4 38.4 1.0
CB F:SER358 4.5 40.6 1.0
CA F:SER358 4.6 40.6 1.0
C F:CYS365 4.7 38.4 1.0
SG F:CYS362 4.7 38.7 1.0
CB F:LEU407 4.7 42.8 1.0
N F:GLY408 4.8 41.8 1.0
SG F:CYS405 4.8 40.4 1.0
CD2 F:LEU407 4.8 42.8 1.0
SG F:CYS359 4.8 39.3 1.0
CB F:CYS362 4.8 38.7 1.0
N F:GLY360 4.9 37.4 1.0
N F:ARG366 4.9 37.0 1.0
C F:SER358 4.9 40.6 1.0

Iron binding site 9 out of 28 in 8q49

Go back to Iron Binding Sites List in 8q49
Iron binding site 9 out of 28 in the Outward-Facing, OPEN2 Proteoliposome Complex I at 2.6 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, OPEN2 Proteoliposome Complex I at 2.6 A. Initially Purified in Lmng. within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe501

b:40.8
occ:1.00
 FE3 F:SF4501 0.0 40.8 1.0
SG F:CYS405 2.3 40.4 1.0
S1 F:SF4501 2.3 40.8 1.0
S2 F:SF4501 2.3 40.8 1.0
S4 F:SF4501 2.3 40.8 1.0
FE4 F:SF4501 2.7 40.8 1.0
FE2 F:SF4501 2.7 40.8 1.0
FE1 F:SF4501 2.7 40.8 1.0
CB F:CYS405 3.3 40.4 1.0
S3 F:SF4501 3.9 40.8 1.0
N F:CYS405 4.0 40.4 1.0
CD1 F:ILE185 4.0 44.2 1.0
CB F:LEU407 4.0 42.8 1.0
CA F:CYS405 4.1 40.4 1.0
CG F:PRO203 4.2 41.2 1.0
C F:CYS405 4.3 40.4 1.0
O F:CYS405 4.5 40.4 1.0
CD F:PRO203 4.6 41.2 1.0
N F:LEU407 4.6 42.8 1.0
SG F:CYS362 4.8 38.7 1.0
SG F:CYS365 4.8 38.4 1.0
SG F:CYS359 4.8 39.3 1.0
N F:GLY408 4.8 41.8 1.0
CA F:LEU407 4.8 42.8 1.0
CG1 F:ILE185 4.9 44.2 1.0

Iron binding site 10 out of 28 in 8q49

Go back to Iron Binding Sites List in 8q49
Iron binding site 10 out of 28 in the Outward-Facing, OPEN2 Proteoliposome Complex I at 2.6 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, OPEN2 Proteoliposome Complex I at 2.6 A. Initially Purified in Lmng. within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe501

b:40.8
occ:1.00
 FE4 F:SF4501 0.0 40.8 1.0
SG F:CYS362 2.2 38.7 1.0
S2 F:SF4501 2.3 40.8 1.0
S1 F:SF4501 2.3 40.8 1.0
S3 F:SF4501 2.3 40.8 1.0
FE2 F:SF4501 2.7 40.8 1.0
FE1 F:SF4501 2.7 40.8 1.0
FE3 F:SF4501 2.7 40.8 1.0
CB F:CYS362 3.1 38.7 1.0
N F:CYS362 3.6 38.7 1.0
S4 F:SF4501 3.9 40.8 1.0
CA F:CYS362 4.0 38.7 1.0
CB F:ILE404 4.1 38.5 1.0
N F:ILE404 4.1 38.5 1.0
N F:CYS405 4.3 40.4 1.0
CB F:CYS365 4.5 38.4 1.0
CD1 F:ILE404 4.6 38.5 1.0
CA F:ILE404 4.6 38.5 1.0
CB F:GLN361 4.6 37.4 1.0
SG F:CYS365 4.6 38.4 1.0
CB F:THR403 4.7 38.4 1.0
CG1 F:ILE404 4.7 38.5 1.0
C F:GLN361 4.7 37.4 1.0
SG F:CYS405 4.7 40.4 1.0
SG F:CYS359 4.8 39.3 1.0
N F:GLN361 4.9 37.4 1.0
CA F:GLN361 5.0 37.4 1.0
C F:ILE404 5.0 38.5 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 14:27:18 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy