Iron in PDB 8q1u: Inward-Facing, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. Initially Purified in Lmng.
Enzymatic activity of Inward-Facing, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. Initially Purified in Lmng.
All present enzymatic activity of Inward-Facing, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. Initially Purified in Lmng.:
1.6.5.3;
1.6.99.3;
7.1.1.2;
Other elements in 8q1u:
The structure of Inward-Facing, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. Initially Purified in Lmng. also contains other interesting chemical elements:
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, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. Initially Purified in Lmng.
(pdb code 8q1u). 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, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. Initially Purified in Lmng., PDB code: 8q1u:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Iron binding site 1 out
of 28 in 8q1u
Go back to
Iron Binding Sites List in 8q1u
Iron binding site 1 out
of 28 in the Inward-Facing, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. 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 Inward-Facing, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. Initially Purified in Lmng. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe201
b:32.4
occ:1.00
|
FE1
|
B:SF4201
|
0.0
|
32.4
|
1.0
|
SG
|
B:CYS119
|
2.2
|
28.3
|
1.0
|
S3
|
B:SF4201
|
2.3
|
32.4
|
1.0
|
S2
|
B:SF4201
|
2.3
|
32.4
|
1.0
|
S4
|
B:SF4201
|
2.3
|
32.4
|
1.0
|
FE3
|
B:SF4201
|
2.7
|
32.4
|
1.0
|
FE4
|
B:SF4201
|
2.7
|
32.4
|
1.0
|
FE2
|
B:SF4201
|
2.7
|
32.4
|
1.0
|
CB
|
B:CYS119
|
3.2
|
28.3
|
1.0
|
S1
|
B:SF4201
|
3.9
|
32.4
|
1.0
|
N
|
B:CYS119
|
4.0
|
28.3
|
1.0
|
OG1
|
B:THR91
|
4.0
|
29.4
|
1.0
|
CA
|
B:CYS119
|
4.1
|
28.3
|
1.0
|
SG
|
B:CYS149
|
4.4
|
29.6
|
1.0
|
CQ2
|
D:2MR85
|
4.8
|
36.9
|
1.0
|
SG
|
B:CYS54
|
4.8
|
32.7
|
1.0
|
SG
|
B:CYS55
|
4.9
|
32.5
|
1.0
|
CE1
|
B:TYR126
|
4.9
|
23.8
|
1.0
|
|
Iron binding site 2 out
of 28 in 8q1u
Go back to
Iron Binding Sites List in 8q1u
Iron binding site 2 out
of 28 in the Inward-Facing, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. 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 Inward-Facing, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. Initially Purified in Lmng. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe201
b:32.4
occ:1.00
|
FE2
|
B:SF4201
|
0.0
|
32.4
|
1.0
|
SG
|
B:CYS149
|
2.3
|
29.6
|
1.0
|
S1
|
B:SF4201
|
2.3
|
32.4
|
1.0
|
S3
|
B:SF4201
|
2.3
|
32.4
|
1.0
|
S4
|
B:SF4201
|
2.3
|
32.4
|
1.0
|
FE4
|
B:SF4201
|
2.7
|
32.4
|
1.0
|
FE1
|
B:SF4201
|
2.7
|
32.4
|
1.0
|
FE3
|
B:SF4201
|
2.7
|
32.4
|
1.0
|
CB
|
B:CYS149
|
3.4
|
29.6
|
1.0
|
CA
|
B:CYS149
|
3.4
|
29.6
|
1.0
|
C
|
B:CYS149
|
3.7
|
29.6
|
1.0
|
S2
|
B:SF4201
|
3.9
|
32.4
|
1.0
|
N
|
B:PRO150
|
4.1
|
31.1
|
1.0
|
O
|
B:CYS149
|
4.2
|
29.6
|
1.0
|
NE
|
D:ARG105
|
4.5
|
34.6
|
1.0
|
CA
|
B:PRO150
|
4.5
|
31.1
|
1.0
|
CD2
|
D:HIS190
|
4.5
|
35.3
|
1.0
|
SG
|
B:CYS55
|
4.6
|
32.5
|
1.0
|
NE2
|
D:HIS190
|
4.7
|
35.3
|
1.0
|
SG
|
B:CYS119
|
4.7
|
28.3
|
1.0
|
N
|
B:CYS149
|
4.8
|
29.6
|
1.0
|
SG
|
B:CYS54
|
4.8
|
32.7
|
1.0
|
O
|
B:GLY148
|
4.8
|
29.9
|
1.0
|
|
Iron binding site 3 out
of 28 in 8q1u
Go back to
Iron Binding Sites List in 8q1u
Iron binding site 3 out
of 28 in the Inward-Facing, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. 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 Inward-Facing, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. Initially Purified in Lmng. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe201
b:32.4
occ:1.00
|
FE3
|
B:SF4201
|
0.0
|
32.4
|
1.0
|
SG
|
B:CYS54
|
2.3
|
32.7
|
1.0
|
S1
|
B:SF4201
|
2.3
|
32.4
|
1.0
|
S4
|
B:SF4201
|
2.3
|
32.4
|
1.0
|
S2
|
B:SF4201
|
2.3
|
32.4
|
1.0
|
FE1
|
B:SF4201
|
2.7
|
32.4
|
1.0
|
FE4
|
B:SF4201
|
2.7
|
32.4
|
1.0
|
FE2
|
B:SF4201
|
2.7
|
32.4
|
1.0
|
CB
|
B:CYS54
|
3.2
|
32.7
|
1.0
|
CQ2
|
D:2MR85
|
3.8
|
36.9
|
1.0
|
S3
|
B:SF4201
|
3.9
|
32.4
|
1.0
|
N
|
B:CYS54
|
4.0
|
32.7
|
1.0
|
NE2
|
D:HIS190
|
4.1
|
35.3
|
1.0
|
CA
|
B:CYS54
|
4.1
|
32.7
|
1.0
|
N
|
B:CYS55
|
4.2
|
32.5
|
1.0
|
CG
|
D:ARG105
|
4.5
|
34.6
|
1.0
|
C
|
B:CYS54
|
4.6
|
32.7
|
1.0
|
CD2
|
D:HIS190
|
4.7
|
35.3
|
1.0
|
CB
|
B:ALA53
|
4.7
|
31.7
|
1.0
|
SG
|
B:CYS119
|
4.8
|
28.3
|
1.0
|
SG
|
B:CYS55
|
4.8
|
32.5
|
1.0
|
SG
|
B:CYS149
|
4.8
|
29.6
|
1.0
|
NH2
|
D:2MR85
|
4.9
|
36.9
|
1.0
|
|
Iron binding site 4 out
of 28 in 8q1u
Go back to
Iron Binding Sites List in 8q1u
Iron binding site 4 out
of 28 in the Inward-Facing, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. 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 Inward-Facing, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. Initially Purified in Lmng. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe201
b:32.4
occ:1.00
|
FE4
|
B:SF4201
|
0.0
|
32.4
|
1.0
|
S3
|
B:SF4201
|
2.3
|
32.4
|
1.0
|
S2
|
B:SF4201
|
2.3
|
32.4
|
1.0
|
S1
|
B:SF4201
|
2.3
|
32.4
|
1.0
|
SG
|
B:CYS55
|
2.3
|
32.5
|
1.0
|
FE2
|
B:SF4201
|
2.7
|
32.4
|
1.0
|
FE3
|
B:SF4201
|
2.7
|
32.4
|
1.0
|
FE1
|
B:SF4201
|
2.7
|
32.4
|
1.0
|
CB
|
B:CYS55
|
3.3
|
32.5
|
1.0
|
N
|
B:CYS55
|
3.7
|
32.5
|
1.0
|
S4
|
B:SF4201
|
3.9
|
32.4
|
1.0
|
CA
|
B:CYS55
|
3.9
|
32.5
|
1.0
|
CA
|
B:PRO150
|
4.5
|
31.1
|
1.0
|
CB
|
B:PRO150
|
4.6
|
31.1
|
1.0
|
CA
|
B:GLY117
|
4.6
|
29.7
|
1.0
|
SG
|
B:CYS54
|
4.6
|
32.7
|
1.0
|
C
|
B:CYS54
|
4.7
|
32.7
|
1.0
|
CB
|
B:CYS54
|
4.7
|
32.7
|
1.0
|
SG
|
B:CYS119
|
4.7
|
28.3
|
1.0
|
SG
|
B:CYS149
|
4.8
|
29.6
|
1.0
|
CB
|
B:CYS119
|
4.9
|
28.3
|
1.0
|
CA
|
B:CYS149
|
4.9
|
29.6
|
1.0
|
N
|
B:PRO150
|
4.9
|
31.1
|
1.0
|
N
|
B:SER118
|
4.9
|
28.1
|
1.0
|
CA
|
B:GLY90
|
4.9
|
31.0
|
1.0
|
|
Iron binding site 5 out
of 28 in 8q1u
Go back to
Iron Binding Sites List in 8q1u
Iron binding site 5 out
of 28 in the Inward-Facing, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. 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 Inward-Facing, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. Initially Purified in Lmng. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Fe301
b:49.7
occ:1.00
|
FE1
|
E:FES301
|
0.0
|
49.7
|
1.0
|
S2
|
E:FES301
|
2.2
|
49.7
|
1.0
|
S1
|
E:FES301
|
2.2
|
49.7
|
1.0
|
SG
|
E:CYS103
|
2.3
|
49.0
|
1.0
|
SG
|
E:CYS108
|
2.3
|
48.2
|
1.0
|
FE2
|
E:FES301
|
2.7
|
49.7
|
1.0
|
CB
|
E:CYS103
|
3.3
|
49.0
|
1.0
|
CB
|
E:CYS108
|
3.3
|
48.2
|
1.0
|
N
|
E:CYS108
|
4.2
|
48.2
|
1.0
|
CA
|
E:CYS144
|
4.2
|
49.8
|
1.0
|
CA
|
E:CYS108
|
4.3
|
48.2
|
1.0
|
SG
|
E:CYS144
|
4.5
|
49.8
|
1.0
|
N
|
E:LEU145
|
4.6
|
49.6
|
1.0
|
CB
|
E:CYS144
|
4.6
|
49.8
|
1.0
|
CG
|
E:MET153
|
4.7
|
52.0
|
1.0
|
CA
|
E:CYS103
|
4.7
|
49.0
|
1.0
|
OG1
|
E:THR105
|
4.7
|
48.1
|
1.0
|
CB
|
E:THR105
|
4.7
|
48.1
|
1.0
|
O
|
E:ALA147
|
4.7
|
49.8
|
1.0
|
SG
|
E:CYS148
|
4.8
|
52.6
|
1.0
|
N
|
E:THR105
|
4.8
|
48.1
|
1.0
|
CA
|
E:CYS148
|
4.9
|
52.6
|
1.0
|
SD
|
E:MET153
|
4.9
|
52.0
|
1.0
|
C
|
E:CYS103
|
4.9
|
49.0
|
1.0
|
C
|
E:CYS144
|
5.0
|
49.8
|
1.0
|
|
Iron binding site 6 out
of 28 in 8q1u
Go back to
Iron Binding Sites List in 8q1u
Iron binding site 6 out
of 28 in the Inward-Facing, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. 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 Inward-Facing, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. Initially Purified in Lmng. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Fe301
b:49.7
occ:1.00
|
FE2
|
E:FES301
|
0.0
|
49.7
|
1.0
|
S2
|
E:FES301
|
2.2
|
49.7
|
1.0
|
S1
|
E:FES301
|
2.2
|
49.7
|
1.0
|
SG
|
E:CYS144
|
2.3
|
49.8
|
1.0
|
SG
|
E:CYS148
|
2.3
|
52.6
|
1.0
|
FE1
|
E:FES301
|
2.7
|
49.7
|
1.0
|
CB
|
E:CYS144
|
3.3
|
49.8
|
1.0
|
CB
|
E:CYS148
|
3.3
|
52.6
|
1.0
|
CA
|
E:CYS148
|
3.6
|
52.6
|
1.0
|
CA
|
E:CYS144
|
3.8
|
49.8
|
1.0
|
N
|
E:CYS148
|
4.0
|
52.6
|
1.0
|
N
|
E:LEU145
|
4.2
|
49.6
|
1.0
|
N
|
F:GLY103
|
4.2
|
53.9
|
1.0
|
N
|
E:GLY146
|
4.2
|
48.7
|
1.0
|
C
|
E:ALA147
|
4.3
|
49.8
|
1.0
|
SG
|
E:CYS103
|
4.4
|
49.0
|
1.0
|
C
|
E:CYS144
|
4.4
|
49.8
|
1.0
|
O
|
E:ALA147
|
4.4
|
49.8
|
1.0
|
SG
|
E:CYS108
|
4.5
|
48.2
|
1.0
|
N
|
E:ALA147
|
4.6
|
49.8
|
1.0
|
CG
|
E:PRO107
|
4.7
|
46.7
|
1.0
|
CB
|
E:PRO107
|
4.7
|
46.7
|
1.0
|
C
|
E:GLY146
|
4.8
|
48.7
|
1.0
|
CA
|
E:GLY146
|
4.8
|
48.7
|
1.0
|
CA
|
F:GLY103
|
4.9
|
53.9
|
1.0
|
|
Iron binding site 7 out
of 28 in 8q1u
Go back to
Iron Binding Sites List in 8q1u
Iron binding site 7 out
of 28 in the Inward-Facing, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. 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 Inward-Facing, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. Initially Purified in Lmng. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Fe502
b:41.6
occ:1.00
|
FE1
|
F:SF4502
|
0.0
|
41.6
|
1.0
|
S4
|
F:SF4502
|
2.3
|
41.6
|
1.0
|
S2
|
F:SF4502
|
2.3
|
41.6
|
1.0
|
S3
|
F:SF4502
|
2.3
|
41.6
|
1.0
|
SG
|
F:CYS359
|
2.3
|
40.6
|
1.0
|
FE3
|
F:SF4502
|
2.7
|
41.6
|
1.0
|
FE2
|
F:SF4502
|
2.7
|
41.6
|
1.0
|
FE4
|
F:SF4502
|
2.7
|
41.6
|
1.0
|
CB
|
F:CYS359
|
3.4
|
40.6
|
1.0
|
N
|
F:CYS359
|
3.8
|
40.6
|
1.0
|
S1
|
F:SF4502
|
3.9
|
41.6
|
1.0
|
N
|
F:GLN361
|
4.0
|
37.5
|
1.0
|
CA
|
F:CYS359
|
4.0
|
40.6
|
1.0
|
N
|
F:GLY360
|
4.0
|
37.8
|
1.0
|
CB
|
F:GLN361
|
4.2
|
37.5
|
1.0
|
C
|
F:CYS359
|
4.3
|
40.6
|
1.0
|
N
|
F:CYS362
|
4.5
|
38.4
|
1.0
|
CD
|
F:PRO203
|
4.5
|
41.5
|
1.0
|
CA
|
F:GLN361
|
4.6
|
37.5
|
1.0
|
OG
|
F:SER358
|
4.7
|
40.7
|
1.0
|
OE1
|
F:GLN361
|
4.8
|
37.5
|
1.0
|
SG
|
F:CYS365
|
4.8
|
39.8
|
1.0
|
SG
|
F:CYS405
|
4.8
|
42.7
|
1.0
|
SG
|
F:CYS362
|
4.9
|
38.4
|
1.0
|
C
|
F:GLY360
|
4.9
|
37.8
|
1.0
|
CA
|
F:GLY360
|
5.0
|
37.8
|
1.0
|
CG
|
F:PRO203
|
5.0
|
41.5
|
1.0
|
C
|
F:SER358
|
5.0
|
40.7
|
1.0
|
|
Iron binding site 8 out
of 28 in 8q1u
Go back to
Iron Binding Sites List in 8q1u
Iron binding site 8 out
of 28 in the Inward-Facing, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. 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 Inward-Facing, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. Initially Purified in Lmng. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Fe502
b:41.6
occ:1.00
|
FE2
|
F:SF4502
|
0.0
|
41.6
|
1.0
|
SG
|
F:CYS365
|
2.2
|
39.8
|
1.0
|
S3
|
F:SF4502
|
2.3
|
41.6
|
1.0
|
S1
|
F:SF4502
|
2.3
|
41.6
|
1.0
|
S4
|
F:SF4502
|
2.3
|
41.6
|
1.0
|
FE4
|
F:SF4502
|
2.7
|
41.6
|
1.0
|
FE3
|
F:SF4502
|
2.7
|
41.6
|
1.0
|
FE1
|
F:SF4502
|
2.7
|
41.6
|
1.0
|
CB
|
F:CYS365
|
3.1
|
39.8
|
1.0
|
OG
|
F:SER358
|
3.4
|
40.7
|
1.0
|
S2
|
F:SF4502
|
3.9
|
41.6
|
1.0
|
CA
|
F:CYS365
|
4.3
|
39.8
|
1.0
|
CB
|
F:SER358
|
4.4
|
40.7
|
1.0
|
N
|
F:CYS359
|
4.5
|
40.6
|
1.0
|
SG
|
F:CYS362
|
4.5
|
38.4
|
1.0
|
C
|
F:CYS365
|
4.6
|
39.8
|
1.0
|
SG
|
F:CYS405
|
4.7
|
42.7
|
1.0
|
CA
|
F:SER358
|
4.7
|
40.7
|
1.0
|
O
|
F:CYS362
|
4.8
|
38.4
|
1.0
|
SG
|
F:CYS359
|
4.8
|
40.6
|
1.0
|
N
|
F:GLY360
|
4.8
|
37.8
|
1.0
|
N
|
F:ARG366
|
4.9
|
36.9
|
1.0
|
N
|
F:CYS365
|
4.9
|
39.8
|
1.0
|
O
|
F:CYS365
|
5.0
|
39.8
|
1.0
|
|
Iron binding site 9 out
of 28 in 8q1u
Go back to
Iron Binding Sites List in 8q1u
Iron binding site 9 out
of 28 in the Inward-Facing, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. 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 Inward-Facing, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. Initially Purified in Lmng. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Fe502
b:41.6
occ:1.00
|
FE3
|
F:SF4502
|
0.0
|
41.6
|
1.0
|
S1
|
F:SF4502
|
2.3
|
41.6
|
1.0
|
S4
|
F:SF4502
|
2.3
|
41.6
|
1.0
|
S2
|
F:SF4502
|
2.3
|
41.6
|
1.0
|
SG
|
F:CYS405
|
2.3
|
42.7
|
1.0
|
FE1
|
F:SF4502
|
2.7
|
41.6
|
1.0
|
FE2
|
F:SF4502
|
2.7
|
41.6
|
1.0
|
FE4
|
F:SF4502
|
2.7
|
41.6
|
1.0
|
CB
|
F:CYS405
|
3.4
|
42.7
|
1.0
|
S3
|
F:SF4502
|
3.9
|
41.6
|
1.0
|
N
|
F:CYS405
|
4.0
|
42.7
|
1.0
|
CA
|
F:CYS405
|
4.2
|
42.7
|
1.0
|
CB
|
F:LEU407
|
4.3
|
43.5
|
1.0
|
C
|
F:CYS405
|
4.5
|
42.7
|
1.0
|
O
|
F:CYS405
|
4.6
|
42.7
|
1.0
|
CG
|
F:PRO203
|
4.6
|
41.5
|
1.0
|
CD1
|
F:ILE185
|
4.7
|
45.0
|
1.0
|
SG
|
F:CYS365
|
4.8
|
39.8
|
1.0
|
N
|
F:GLY408
|
4.8
|
43.0
|
1.0
|
SG
|
F:CYS359
|
4.8
|
40.6
|
1.0
|
SG
|
F:CYS362
|
4.9
|
38.4
|
1.0
|
N
|
F:LEU407
|
4.9
|
43.5
|
1.0
|
CD
|
F:PRO203
|
5.0
|
41.5
|
1.0
|
|
Iron binding site 10 out
of 28 in 8q1u
Go back to
Iron Binding Sites List in 8q1u
Iron binding site 10 out
of 28 in the Inward-Facing, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. 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 Inward-Facing, OPEN1 Proteoliposome Complex I at 3.3 A, After Deactivation Treatment. Initially Purified in Lmng. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Fe502
b:41.6
occ:1.00
|
FE4
|
F:SF4502
|
0.0
|
41.6
|
1.0
|
S1
|
F:SF4502
|
2.3
|
41.6
|
1.0
|
S3
|
F:SF4502
|
2.3
|
41.6
|
1.0
|
SG
|
F:CYS362
|
2.3
|
38.4
|
1.0
|
S2
|
F:SF4502
|
2.3
|
41.6
|
1.0
|
FE2
|
F:SF4502
|
2.7
|
41.6
|
1.0
|
FE3
|
F:SF4502
|
2.7
|
41.6
|
1.0
|
FE1
|
F:SF4502
|
2.7
|
41.6
|
1.0
|
CB
|
F:CYS362
|
3.3
|
38.4
|
1.0
|
N
|
F:CYS362
|
3.8
|
38.4
|
1.0
|
S4
|
F:SF4502
|
3.9
|
41.6
|
1.0
|
CA
|
F:CYS362
|
4.0
|
38.4
|
1.0
|
O
|
F:CYS362
|
4.1
|
38.4
|
1.0
|
N
|
F:ILE404
|
4.4
|
40.5
|
1.0
|
C
|
F:CYS362
|
4.4
|
38.4
|
1.0
|
CB
|
F:CYS365
|
4.5
|
39.8
|
1.0
|
CB
|
F:ILE404
|
4.6
|
40.5
|
1.0
|
SG
|
F:CYS365
|
4.6
|
39.8
|
1.0
|
CB
|
F:THR403
|
4.6
|
40.2
|
1.0
|
CG1
|
F:ILE404
|
4.7
|
40.5
|
1.0
|
SG
|
F:CYS359
|
4.8
|
40.6
|
1.0
|
N
|
F:CYS405
|
4.8
|
42.7
|
1.0
|
SG
|
F:CYS405
|
4.8
|
42.7
|
1.0
|
CD1
|
F:ILE404
|
4.9
|
40.5
|
1.0
|
CG2
|
F:THR403
|
4.9
|
40.2
|
1.0
|
C
|
F:GLN361
|
4.9
|
37.5
|
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 13:36:30 2024
|