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7DGR

Activity optimized supercomplex state2

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
10003954molecular_functionNADH dehydrogenase activity
10005743cellular_componentmitochondrial inner membrane
10008137molecular_functionNADH dehydrogenase (ubiquinone) activity
10009060biological_processaerobic respiration
10016020cellular_componentmembrane
10022904biological_processrespiratory electron transport chain
10032981biological_processmitochondrial respiratory chain complex I assembly
10045271cellular_componentrespiratory chain complex I
11902600biological_processproton transmembrane transport
20005743cellular_componentmitochondrial inner membrane
20006120biological_processmitochondrial electron transport, NADH to ubiquinone
20008137molecular_functionNADH dehydrogenase (ubiquinone) activity
20022904biological_processrespiratory electron transport chain
20032981biological_processmitochondrial respiratory chain complex I assembly
20045271cellular_componentrespiratory chain complex I
21902600biological_processproton transmembrane transport
30005743cellular_componentmitochondrial inner membrane
30006120biological_processmitochondrial electron transport, NADH to ubiquinone
30008137molecular_functionNADH dehydrogenase (ubiquinone) activity
30022904biological_processrespiratory electron transport chain
30045271cellular_componentrespiratory chain complex I
31902600biological_processproton transmembrane transport
40003954molecular_functionNADH dehydrogenase activity
40005743cellular_componentmitochondrial inner membrane
40006120biological_processmitochondrial electron transport, NADH to ubiquinone
40008137molecular_functionNADH dehydrogenase (ubiquinone) activity
40009060biological_processaerobic respiration
40015990biological_processelectron transport coupled proton transport
40022904biological_processrespiratory electron transport chain
40032981biological_processmitochondrial respiratory chain complex I assembly
40042773biological_processATP synthesis coupled electron transport
40045271cellular_componentrespiratory chain complex I
40048039molecular_functionubiquinone binding
50005743cellular_componentmitochondrial inner membrane
50008137molecular_functionNADH dehydrogenase (ubiquinone) activity
50016651molecular_functionoxidoreductase activity, acting on NAD(P)H
50022904biological_processrespiratory electron transport chain
50042773biological_processATP synthesis coupled electron transport
50045271cellular_componentrespiratory chain complex I
51902600biological_processproton transmembrane transport
60005743cellular_componentmitochondrial inner membrane
60006120biological_processmitochondrial electron transport, NADH to ubiquinone
60008137molecular_functionNADH dehydrogenase (ubiquinone) activity
60015990biological_processelectron transport coupled proton transport
60022904biological_processrespiratory electron transport chain
60032981biological_processmitochondrial respiratory chain complex I assembly
60042773biological_processATP synthesis coupled electron transport
60045271cellular_componentrespiratory chain complex I
70005739cellular_componentmitochondrion
70005743cellular_componentmitochondrial inner membrane
70006120biological_processmitochondrial electron transport, NADH to ubiquinone
70008137molecular_functionNADH dehydrogenase (ubiquinone) activity
70022904biological_processrespiratory electron transport chain
70032981biological_processmitochondrial respiratory chain complex I assembly
70045271cellular_componentrespiratory chain complex I
71902600biological_processproton transmembrane transport
80005743cellular_componentmitochondrial inner membrane
80006120biological_processmitochondrial electron transport, NADH to ubiquinone
80008137molecular_functionNADH dehydrogenase (ubiquinone) activity
80010181molecular_functionFMN binding
80016491molecular_functionoxidoreductase activity
80022904biological_processrespiratory electron transport chain
80045271cellular_componentrespiratory chain complex I
80046872molecular_functionmetal ion binding
80051287molecular_functionNAD binding
80051536molecular_functioniron-sulfur cluster binding
80051539molecular_function4 iron, 4 sulfur cluster binding
81902600biological_processproton transmembrane transport
90016491molecular_functionoxidoreductase activity
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005758cellular_componentmitochondrial intermembrane space
A0006120biological_processmitochondrial electron transport, NADH to ubiquinone
A0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
A0009055molecular_functionelectron transfer activity
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016651molecular_functionoxidoreductase activity, acting on NAD(P)H
A0022904biological_processrespiratory electron transport chain
A0032981biological_processmitochondrial respiratory chain complex I assembly
A0042773biological_processATP synthesis coupled electron transport
A0045271cellular_componentrespiratory chain complex I
A0045333biological_processcellular respiration
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
A1902600biological_processproton transmembrane transport
A00008121molecular_functionquinol-cytochrome-c reductase activity
A00016020cellular_componentmembrane
A00051537molecular_function2 iron, 2 sulfur cluster binding
A10005743cellular_componentmitochondrial inner membrane
A10006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
A10016020cellular_componentmembrane
A10022904biological_processrespiratory electron transport chain
A10045275cellular_componentrespiratory chain complex III
A20005739cellular_componentmitochondrion
A20005743cellular_componentmitochondrial inner membrane
A20006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
A20016020cellular_componentmembrane
A20021539biological_processsubthalamus development
A20021548biological_processpons development
A20021680biological_processcerebellar Purkinje cell layer development
A20021766biological_processhippocampus development
A20021794biological_processthalamus development
A20021854biological_processhypothalamus development
A20021860biological_processpyramidal neuron development
A20022904biological_processrespiratory electron transport chain
A20030901biological_processmidbrain development
A20045275cellular_componentrespiratory chain complex III
A30005739cellular_componentmitochondrion
A30005743cellular_componentmitochondrial inner membrane
A30006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
A30022904biological_processrespiratory electron transport chain
A30045275cellular_componentrespiratory chain complex III
A40005743cellular_componentmitochondrial inner membrane
A40006119biological_processoxidative phosphorylation
A40006123biological_processmitochondrial electron transport, cytochrome c to oxygen
A40016491molecular_functionoxidoreductase activity
A40030234molecular_functionenzyme regulator activity
A40045277cellular_componentrespiratory chain complex IV
A50005739cellular_componentmitochondrion
A50005743cellular_componentmitochondrial inner membrane
A50006119biological_processoxidative phosphorylation
A50016020cellular_componentmembrane
A50045277cellular_componentrespiratory chain complex IV
A60005739cellular_componentmitochondrion
A60005740cellular_componentmitochondrial envelope
A60005743cellular_componentmitochondrial inner membrane
A60006119biological_processoxidative phosphorylation
A60006123biological_processmitochondrial electron transport, cytochrome c to oxygen
A60045277cellular_componentrespiratory chain complex IV
A60046872molecular_functionmetal ion binding
A70005743cellular_componentmitochondrial inner membrane
A70006119biological_processoxidative phosphorylation
A70006123biological_processmitochondrial electron transport, cytochrome c to oxygen
A70045277cellular_componentrespiratory chain complex IV
A80005739cellular_componentmitochondrion
A80005743cellular_componentmitochondrial inner membrane
A80006119biological_processoxidative phosphorylation
A80006123biological_processmitochondrial electron transport, cytochrome c to oxygen
A80045277cellular_componentrespiratory chain complex IV
A90004129molecular_functioncytochrome-c oxidase activity
A90005743cellular_componentmitochondrial inner membrane
A90006119biological_processoxidative phosphorylation
A90009060biological_processaerobic respiration
A90016020cellular_componentmembrane
A90020037molecular_functionheme binding
A90022904biological_processrespiratory electron transport chain
A90045277cellular_componentrespiratory chain complex IV
A90046872molecular_functionmetal ion binding
A91902600biological_processproton transmembrane transport
B0003954molecular_functionNADH dehydrogenase activity
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0006120biological_processmitochondrial electron transport, NADH to ubiquinone
B0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
B0016491molecular_functionoxidoreductase activity
B0016651molecular_functionoxidoreductase activity, acting on NAD(P)H
B0019826molecular_functionoxygen sensor activity
B0022008biological_processneurogenesis
B0022904biological_processrespiratory electron transport chain
B0032981biological_processmitochondrial respiratory chain complex I assembly
B0042063biological_processgliogenesis
B0045271cellular_componentrespiratory chain complex I
B0046872molecular_functionmetal ion binding
B0048038molecular_functionquinone binding
B0051287molecular_functionNAD binding
B0051536molecular_functioniron-sulfur cluster binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
B0061351biological_processneural precursor cell proliferation
B0071453biological_processcellular response to oxygen levels
B1902600biological_processproton transmembrane transport
B00005739cellular_componentmitochondrion
B00005743cellular_componentmitochondrial inner membrane
B00006119biological_processoxidative phosphorylation
B00006123biological_processmitochondrial electron transport, cytochrome c to oxygen
B00007417biological_processcentral nervous system development
B00016020cellular_componentmembrane
B00045277cellular_componentrespiratory chain complex IV
B10008121molecular_functionquinol-cytochrome-c reductase activity
B20005739cellular_componentmitochondrion
B20005743cellular_componentmitochondrial inner membrane
B20006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
B20016020cellular_componentmembrane
B20022904biological_processrespiratory electron transport chain
B20045275cellular_componentrespiratory chain complex III
B30005743cellular_componentmitochondrial inner membrane
B30006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
B30016020cellular_componentmembrane
B30022904biological_processrespiratory electron transport chain
B30045275cellular_componentrespiratory chain complex III
B30098803cellular_componentrespiratory chain complex
B40005743cellular_componentmitochondrial inner membrane
B40006119biological_processoxidative phosphorylation
B40016020cellular_componentmembrane
B40045277cellular_componentrespiratory chain complex IV
C0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
C0016651molecular_functionoxidoreductase activity, acting on NAD(P)H
C00004129molecular_functioncytochrome-c oxidase activity
C00005739cellular_componentmitochondrion
C00005743cellular_componentmitochondrial inner membrane
C00006119biological_processoxidative phosphorylation
C00006123biological_processmitochondrial electron transport, cytochrome c to oxygen
C00045277cellular_componentrespiratory chain complex IV
C00046872molecular_functionmetal ion binding
C01902600biological_processproton transmembrane transport
C10005743cellular_componentmitochondrial inner membrane
C10006119biological_processoxidative phosphorylation
C10006123biological_processmitochondrial electron transport, cytochrome c to oxygen
C10045277cellular_componentrespiratory chain complex IV
C20004129molecular_functioncytochrome-c oxidase activity
C20005739cellular_componentmitochondrion
C20005743cellular_componentmitochondrial inner membrane
C20006123biological_processmitochondrial electron transport, cytochrome c to oxygen
C20008535biological_processrespiratory chain complex IV assembly
C20009055molecular_functionelectron transfer activity
C20016020cellular_componentmembrane
C20019646biological_processaerobic electron transport chain
C20022904biological_processrespiratory electron transport chain
C20045277cellular_componentrespiratory chain complex IV
C21902600biological_processproton transmembrane transport
C30005739cellular_componentmitochondrion
C30005743cellular_componentmitochondrial inner membrane
C30006119biological_processoxidative phosphorylation
C30006123biological_processmitochondrial electron transport, cytochrome c to oxygen
C30016491molecular_functionoxidoreductase activity
C30030674molecular_functionprotein-macromolecule adaptor activity
C30031966cellular_componentmitochondrial membrane
C30045277cellular_componentrespiratory chain complex IV
C30097250biological_processmitochondrial respirasome assembly
C30098803cellular_componentrespiratory chain complex
C40004129molecular_functioncytochrome-c oxidase activity
C40005507molecular_functioncopper ion binding
C40005739cellular_componentmitochondrion
C40005743cellular_componentmitochondrial inner membrane
C40016020cellular_componentmembrane
C40016491molecular_functionoxidoreductase activity
C40017004biological_processcytochrome complex assembly
C40022900biological_processelectron transport chain
C40022904biological_processrespiratory electron transport chain
C40031966cellular_componentmitochondrial membrane
C40042773biological_processATP synthesis coupled electron transport
C40045277cellular_componentrespiratory chain complex IV
C40046872molecular_functionmetal ion binding
C41902600biological_processproton transmembrane transport
D0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
D0048038molecular_functionquinone binding
D0051536molecular_functioniron-sulfur cluster binding
D0051539molecular_function4 iron, 4 sulfur cluster binding
E0016020cellular_componentmembrane
E0016651molecular_functionoxidoreductase activity, acting on NAD(P)H
E0051539molecular_function4 iron, 4 sulfur cluster binding
F0005739cellular_componentmitochondrion
F0045271cellular_componentrespiratory chain complex I
G0022900biological_processelectron transport chain
H0005739cellular_componentmitochondrion
H0005743cellular_componentmitochondrial inner membrane
H0005758cellular_componentmitochondrial intermembrane space
H0022904biological_processrespiratory electron transport chain
H0032981biological_processmitochondrial respiratory chain complex I assembly
H0045271cellular_componentrespiratory chain complex I
I0006120biological_processmitochondrial electron transport, NADH to ubiquinone
J0005739cellular_componentmitochondrion
J0005743cellular_componentmitochondrial inner membrane
J0022904biological_processrespiratory electron transport chain
J0045271cellular_componentrespiratory chain complex I
K0005739cellular_componentmitochondrion
K0005743cellular_componentmitochondrial inner membrane
K0022904biological_processrespiratory electron transport chain
K0031966cellular_componentmitochondrial membrane
K0045271cellular_componentrespiratory chain complex I
L0005739cellular_componentmitochondrion
L0005743cellular_componentmitochondrial inner membrane
L0022904biological_processrespiratory electron transport chain
L0045271cellular_componentrespiratory chain complex I
M0006633biological_processfatty acid biosynthetic process
N0005739cellular_componentmitochondrion
N0005743cellular_componentmitochondrial inner membrane
N0022904biological_processrespiratory electron transport chain
N0045271cellular_componentrespiratory chain complex I
O0005739cellular_componentmitochondrion
O0005743cellular_componentmitochondrial inner membrane
O0022904biological_processrespiratory electron transport chain
O0032981biological_processmitochondrial respiratory chain complex I assembly
O0045271cellular_componentrespiratory chain complex I
P0005739cellular_componentmitochondrion
P0005743cellular_componentmitochondrial inner membrane
P0006120biological_processmitochondrial electron transport, NADH to ubiquinone
P0016491molecular_functionoxidoreductase activity
P0022904biological_processrespiratory electron transport chain
P0042773biological_processATP synthesis coupled electron transport
P0045271cellular_componentrespiratory chain complex I
Q0005739cellular_componentmitochondrion
Q0005743cellular_componentmitochondrial inner membrane
Q0005758cellular_componentmitochondrial intermembrane space
Q0006120biological_processmitochondrial electron transport, NADH to ubiquinone
Q0022904biological_processrespiratory electron transport chain
Q0045271cellular_componentrespiratory chain complex I
R0003954molecular_functionNADH dehydrogenase activity
R0005739cellular_componentmitochondrion
R0005743cellular_componentmitochondrial inner membrane
R0005759cellular_componentmitochondrial matrix
R0006744biological_processubiquinone biosynthetic process
R0007623biological_processcircadian rhythm
R0022904biological_processrespiratory electron transport chain
R0031966cellular_componentmitochondrial membrane
R0044877molecular_functionprotein-containing complex binding
R0045271cellular_componentrespiratory chain complex I
S0005737cellular_componentcytoplasm
S0005739cellular_componentmitochondrion
S0005759cellular_componentmitochondrial matrix
S0006120biological_processmitochondrial electron transport, NADH to ubiquinone
S0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
S0022904biological_processrespiratory electron transport chain
S0045271cellular_componentrespiratory chain complex I
S1902600biological_processproton transmembrane transport
T0005739cellular_componentmitochondrion
T0005743cellular_componentmitochondrial inner membrane
T0006120biological_processmitochondrial electron transport, NADH to ubiquinone
T0022904biological_processrespiratory electron transport chain
T0045271cellular_componentrespiratory chain complex I
U0005739cellular_componentmitochondrion
U0005743cellular_componentmitochondrial inner membrane
U0016020cellular_componentmembrane
U0022904biological_processrespiratory electron transport chain
U0045271cellular_componentrespiratory chain complex I
V0005634cellular_componentnucleus
V0005654cellular_componentnucleoplasm
V0005737cellular_componentcytoplasm
V0005739cellular_componentmitochondrion
V0005743cellular_componentmitochondrial inner membrane
V0006915biological_processapoptotic process
V0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
V0022904biological_processrespiratory electron transport chain
V0045271cellular_componentrespiratory chain complex I
V0045892biological_processnegative regulation of DNA-templated transcription
V1902600biological_processproton transmembrane transport
W0006633biological_processfatty acid biosynthetic process
X0005739cellular_componentmitochondrion
X0005743cellular_componentmitochondrial inner membrane
X0022904biological_processrespiratory electron transport chain
X0045271cellular_componentrespiratory chain complex I
Y0005743cellular_componentmitochondrial inner membrane
Y0045271cellular_componentrespiratory chain complex I
Z0005739cellular_componentmitochondrion
Z0005743cellular_componentmitochondrial inner membrane
Z0022900biological_processelectron transport chain
Z0022904biological_processrespiratory electron transport chain
Z0045271cellular_componentrespiratory chain complex I
a0005739cellular_componentmitochondrion
a0005743cellular_componentmitochondrial inner membrane
a0022904biological_processrespiratory electron transport chain
a0045271cellular_componentrespiratory chain complex I
c0005739cellular_componentmitochondrion
c0005743cellular_componentmitochondrial inner membrane
c0006120biological_processmitochondrial electron transport, NADH to ubiquinone
c0022904biological_processrespiratory electron transport chain
c0042775biological_processmitochondrial ATP synthesis coupled electron transport
c0045271cellular_componentrespiratory chain complex I
d0005739cellular_componentmitochondrion
e0005739cellular_componentmitochondrion
e0006120biological_processmitochondrial electron transport, NADH to ubiquinone
f0005739cellular_componentmitochondrion
f0005743cellular_componentmitochondrial inner membrane
f0006120biological_processmitochondrial electron transport, NADH to ubiquinone
f0022904biological_processrespiratory electron transport chain
f0045271cellular_componentrespiratory chain complex I
g0005739cellular_componentmitochondrion
g0005743cellular_componentmitochondrial inner membrane
g0022904biological_processrespiratory electron transport chain
g0045271cellular_componentrespiratory chain complex I
i0005739cellular_componentmitochondrion
i0045271cellular_componentrespiratory chain complex I
j0005737cellular_componentcytoplasm
j0005739cellular_componentmitochondrion
j0005743cellular_componentmitochondrial inner membrane
j0006120biological_processmitochondrial electron transport, NADH to ubiquinone
j0022904biological_processrespiratory electron transport chain
j0032981biological_processmitochondrial respiratory chain complex I assembly
j0045271cellular_componentrespiratory chain complex I
k0005739cellular_componentmitochondrion
k0005743cellular_componentmitochondrial inner membrane
k0006627biological_processprotein processing involved in protein targeting to mitochondrion
k0016020cellular_componentmembrane
k0017087cellular_componentmitochondrial processing peptidase complex
k0022904biological_processrespiratory electron transport chain
k0032991cellular_componentprotein-containing complex
k0046872molecular_functionmetal ion binding
l0004222molecular_functionmetalloendopeptidase activity
l0005739cellular_componentmitochondrion
l0005743cellular_componentmitochondrial inner membrane
l0006508biological_processproteolysis
l0022904biological_processrespiratory electron transport chain
l0045275cellular_componentrespiratory chain complex III
l0046872molecular_functionmetal ion binding
m0005739cellular_componentmitochondrion
m0005743cellular_componentmitochondrial inner membrane
m0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
m0008121molecular_functionquinol-cytochrome-c reductase activity
m0009055molecular_functionelectron transfer activity
m0016020cellular_componentmembrane
m0016491molecular_functionoxidoreductase activity
m0020037molecular_functionheme binding
m0022904biological_processrespiratory electron transport chain
m0031966cellular_componentmitochondrial membrane
m0045275cellular_componentrespiratory chain complex III
m0046872molecular_functionmetal ion binding
m0048039molecular_functionubiquinone binding
m1902600biological_processproton transmembrane transport
o0009055molecular_functionelectron transfer activity
o0020037molecular_functionheme binding
p0008121molecular_functionquinol-cytochrome-c reductase activity
p0016020cellular_componentmembrane
p0051537molecular_function2 iron, 2 sulfur cluster binding
q0005743cellular_componentmitochondrial inner membrane
q0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
q0016020cellular_componentmembrane
q0022904biological_processrespiratory electron transport chain
q0045275cellular_componentrespiratory chain complex III
r0005739cellular_componentmitochondrion
r0005743cellular_componentmitochondrial inner membrane
r0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
r0016020cellular_componentmembrane
r0021539biological_processsubthalamus development
r0021548biological_processpons development
r0021680biological_processcerebellar Purkinje cell layer development
r0021766biological_processhippocampus development
r0021794biological_processthalamus development
r0021854biological_processhypothalamus development
r0021860biological_processpyramidal neuron development
r0022904biological_processrespiratory electron transport chain
r0030901biological_processmidbrain development
r0045275cellular_componentrespiratory chain complex III
s0005743cellular_componentmitochondrial inner membrane
s0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
s0016020cellular_componentmembrane
s0022904biological_processrespiratory electron transport chain
s0045275cellular_componentrespiratory chain complex III
s0098803cellular_componentrespiratory chain complex
t0005739cellular_componentmitochondrion
t0005743cellular_componentmitochondrial inner membrane
t0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
t0022904biological_processrespiratory electron transport chain
t0045275cellular_componentrespiratory chain complex III
u0005739cellular_componentmitochondrion
u0005743cellular_componentmitochondrial inner membrane
u0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
u0016020cellular_componentmembrane
u0022904biological_processrespiratory electron transport chain
u0045275cellular_componentrespiratory chain complex III
v0008121molecular_functionquinol-cytochrome-c reductase activity
w0005739cellular_componentmitochondrion
w0005743cellular_componentmitochondrial inner membrane
w0006627biological_processprotein processing involved in protein targeting to mitochondrion
w0016020cellular_componentmembrane
w0017087cellular_componentmitochondrial processing peptidase complex
w0022904biological_processrespiratory electron transport chain
w0032991cellular_componentprotein-containing complex
w0046872molecular_functionmetal ion binding
x0004222molecular_functionmetalloendopeptidase activity
x0005739cellular_componentmitochondrion
x0005743cellular_componentmitochondrial inner membrane
x0006508biological_processproteolysis
x0022904biological_processrespiratory electron transport chain
x0045275cellular_componentrespiratory chain complex III
x0046872molecular_functionmetal ion binding
y0005739cellular_componentmitochondrion
y0005743cellular_componentmitochondrial inner membrane
y0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
y0008121molecular_functionquinol-cytochrome-c reductase activity
y0009055molecular_functionelectron transfer activity
y0016020cellular_componentmembrane
y0016491molecular_functionoxidoreductase activity
y0020037molecular_functionheme binding
y0022904biological_processrespiratory electron transport chain
y0031966cellular_componentmitochondrial membrane
y0045275cellular_componentrespiratory chain complex III
y0046872molecular_functionmetal ion binding
y0048039molecular_functionubiquinone binding
y1902600biological_processproton transmembrane transport
z0009055molecular_functionelectron transfer activity
z0020037molecular_functionheme binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue FES 9 301
ChainResidue
9CYS135
9THR137
9CYS140
9CYS176
9LEU177
9ALA179
9CYS180

site_idAC2
Number of Residues6
Detailsbinding site for residue 3PE 4 501
ChainResidue
4PRO13
4TRP16
4THR90
jLEU43
2PRO238
4MET12

site_idAC3
Number of Residues7
Detailsbinding site for residue CDL 4 502
ChainResidue
4LEU446
4LEU447
4LEU449
6MET20
6SER23
6TRP66
hALA107

site_idAC4
Number of Residues6
Detailsbinding site for residue 3PE 4 503
ChainResidue
2ILE276
2ILE277
4ALA163
4TYR166
4ALA198
TTRP133

site_idAC5
Number of Residues4
Detailsbinding site for residue PC1 4 504
ChainResidue
4LEU2
4ILE5
4LEU55
4PHE105

site_idAC6
Number of Residues10
Detailsbinding site for residue 3PE 2 401
ChainResidue
2LYS322
2THR324
2PHE325
2LEU326
2MET329
jLEU63
jTYR64
jSER67
jPHE68
jVAL71

site_idAC7
Number of Residues10
Detailsbinding site for residue PC1 2 402
ChainResidue
2SER126
2ILE129
2ILE210
2SER213
2THR217
2LEU319
2LYS321
2LYS322
2LEU326
SASN294

site_idAC8
Number of Residues16
Detailsbinding site for residue CDL 6 701
ChainResidue
4GLN349
4PRO353
4LEU360
4LEU364
6ILE19
6MET22
6SER23
6LYS116
6LYS119
6TYR120
6LEU123
6ILE149
6MET150
6LEU153
6TYR159
bLEU68

site_idAC9
Number of Residues13
Detailsbinding site for residue FMN 8 501
ChainResidue
8GLY89
8LYS98
8ASN116
8ASP118
8GLU119
8GLY120
8CYS206
8GLY207
8GLU208
8GLU209
8VAL242
8ALA243
8ASN244

site_idAD1
Number of Residues8
Detailsbinding site for residue SF4 8 502
ChainResidue
8TYR204
8SER378
8CYS379
8GLY380
8GLN381
8CYS382
8CYS385
8CYS425

site_idAD2
Number of Residues7
Detailsbinding site for residue SF4 A 801
ChainResidue
AHIS124
AASP127
ACYS128
ACYS131
ACYS137
AGLN140
AARG175

site_idAD3
Number of Residues6
Detailsbinding site for residue SF4 A 802
ChainResidue
ALEU231
ACYS176
AGLN178
ACYS182
ACYS226
AALA230

site_idAD4
Number of Residues9
Detailsbinding site for residue FES A 803
ChainResidue
APHE63
ACYS64
ATYR65
AALA72
AGLY73
AASN74
ACYS75
ACYS78
ACYS92

site_idAD5
Number of Residues11
Detailsbinding site for residue 3PE B 501
ChainResidue
1MET183
1LEU296
BARG266
BILE267
ELEU61
ETRP63
LVAL18
LALA21
LILE25
LLEU28
VPHE36

site_idAD6
Number of Residues5
Detailsbinding site for residue SF4 D 301
ChainResidue
DALA90
DCYS91
DCYS92
DCYS156
DCYS186

site_idAD7
Number of Residues8
Detailsbinding site for residue SF4 E 301
ChainResidue
ECYS123
EPRO124
ECYS152
EILE153
ETYR154
ECYS155
ECYS158
EGLU169

site_idAD8
Number of Residues8
Detailsbinding site for residue SF4 E 302
ChainResidue
ECYS113
EILE114
ECYS116
ELYS117
ECYS119
ETYR145
ECYS162
EALA166

site_idAD9
Number of Residues5
Detailsbinding site for residue ZN I 300
ChainResidue
ICYS87
IASP88
IGLY89
IHIS96
ICYS115

site_idAE1
Number of Residues11
Detailsbinding site for residue CDL J 101
ChainResidue
JPHE3
JLEU6
PARG6
PPHE7
PILE8
UGLU2
ULEU3
UVAL6
ULEU7
UGLN13
UARG34

site_idAE2
Number of Residues6
Detailsbinding site for residue PC1 L 200
ChainResidue
3TRP106
LPHE8
LLEU9
LGLU16
LLEU19
LPHE23

site_idAE3
Number of Residues12
Detailsbinding site for residue NAP R 601
ChainResidue
DARG215
RGLY63
RPHE64
RLEU65
RARG85
RLEU129
RVAL130
RGLY131
RARG132
RTYR180
RALA204
RILE206

site_idAE4
Number of Residues6
Detailsbinding site for residue PC1 S 401
ChainResidue
2ILE4
STYR31
SGLU35
SMET284
SLEU285
SVAL286

site_idAE5
Number of Residues4
Detailsbinding site for residue PC1 j 201
ChainResidue
2VAL345
jPHE11
jGLN12
jPHE13

site_idAE6
Number of Residues10
Detailsbinding site for residue HEM m 401
ChainResidue
mLEU41
mILE45
mGLY48
mLEU49
mHIS83
mALA84
mLEU133
mPRO134
mHIS182
mPHE183

site_idAE7
Number of Residues12
Detailsbinding site for residue HEM m 402
ChainResidue
mTRP31
mGLY34
mHIS97
mARG100
mSER106
mGLY116
mLEU119
mLEU120
mHIS196
mLEU200
mSER205
mASN206

site_idAE8
Number of Residues11
Detailsbinding site for residue HEC o 301
ChainResidue
oVAL36
oCYS37
oSER39
oCYS40
oHIS41
oASN105
oPRO110
oARG120
oGLY159
oMET160
oPRO163

site_idAE9
Number of Residues10
Detailsbinding site for residue HEM y 401
ChainResidue
yLEU41
yILE45
yGLY48
yLEU49
yHIS83
yALA84
yLEU133
yPRO134
yHIS182
yPHE183

site_idAF1
Number of Residues12
Detailsbinding site for residue HEM y 402
ChainResidue
yTRP31
yGLY34
yHIS97
yARG100
ySER106
yGLY116
yLEU119
yLEU120
yHIS196
yLEU200
ySER205
yASN206

site_idAF2
Number of Residues11
Detailsbinding site for residue HEC z 301
ChainResidue
zVAL36
zCYS37
zSER39
zCYS40
zHIS41
zASN105
zPRO110
zARG120
zGLY159
zMET160
zPRO163

site_idAF3
Number of Residues23
Detailsbinding site for residue HEA A9 601
ChainResidue
A9GLY27
A9MET28
A9SER34
A9ILE37
A9ARG38
A9TYR54
A9VAL58
A9HIS61
A9ALA62
A9MET65
A9ILE66
A9VAL70
A9GLY125
A9TRP126
A9TYR371
A9PHE377
A9HIS378
A9SER382
A9PHE425
A9GLN428
A9ARG438
A9ARG439
A9MET468

site_idAF4
Number of Residues22
Detailsbinding site for residue HEA A9 602
ChainResidue
A9TRP126
A9TRP236
A9VAL243
A9TYR244
A9HIS290
A9HIS291
A9THR309
A9ALA313
A9THR316
A9GLY317
A9GLY352
A9LEU353
A9GLY355
A9ILE356
A9LEU358
A9ALA359
A9ASP364
A9HIS368
A9HIS376
A9PHE377
A9VAL380
A9ARG438

site_idAF5
Number of Residues3
Detailsbinding site for residue CU A9 603
ChainResidue
A9HIS240
A9HIS290
A9HIS291

site_idAF6
Number of Residues3
Detailsbinding site for residue MG A9 604
ChainResidue
A9HIS368
A9ASP369
C4GLU198

site_idAF7
Number of Residues5
Detailsbinding site for residue CU C4 301
ChainResidue
C4HIS161
C4CYS196
C4CYS200
C4MET207
C4CU302

site_idAF8
Number of Residues5
Detailsbinding site for residue CU C4 302
ChainResidue
C4CYS196
C4GLU198
C4CYS200
C4HIS204
C4CU301

site_idAF9
Number of Residues4
Detailsbinding site for residue ZN A6 101
ChainResidue
A6CYS60
A6CYS62
A6CYS82
A6CYS85

Functional Information from PROSITE/UniProt
site_idPS00012
Number of Residues16
DetailsPHOSPHOPANTETHEINE Phosphopantetheine attachment site. DLGLDSLDQVEIIMAM
ChainResidueDetails
WASP107-MET122

site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DIDAEKLMCpqEI
ChainResidueDetails
WASP132-ILE144

site_idPS00077
Number of Residues56
DetailsCOX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WFFGHPeVyililpgfgmishivtyysgkkepfgymgmvwammsigflgfivwa.HH
ChainResidueDetails
A9TRP236-HIS291

site_idPS00078
Number of Residues49
DetailsCOX2 CO II and nitrous oxide reductase dinuclear copper centers signature. VlHswavpslglktdaipgrlnqttlmssrpglyygq......CseiCgsnHsfM
ChainResidueDetails
C4VAL159-MET207

site_idPS00143
Number of Residues24
DetailsINSULINASE Insulinase family, zinc-binding region signature. GsryensnnlGtSHLLRLAsSlTT
ChainResidueDetails
xGLY54-THR77

site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiACKlCEaVCP
ChainResidueDetails
ECYS113-PRO124
ECYS152-PRO163

site_idPS00535
Number of Residues12
DetailsCOMPLEX1_49K Respiratory chain NADH dehydrogenase 49 Kd subunit signature. LHRGtEKLiEyK
ChainResidueDetails
BLEU116-LYS127

site_idPS00542
Number of Residues22
DetailsCOMPLEX1_30K Respiratory chain NADH dehydrogenase 30 Kd subunit signature. EREiwDMFgvffanHpdlRrIL
ChainResidueDetails
CGLU169-LEU190

site_idPS00641
Number of Residues18
DetailsCOMPLEX1_75K_1 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 1. PrfCYherlsvaGnCRmC
ChainResidueDetails
APRO61-CYS78

site_idPS00642
Number of Residues13
DetailsCOMPLEX1_75K_2 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 2. CPiCDqGGeCdLQ
ChainResidueDetails
ACYS128-GLN140

site_idPS00643
Number of Residues11
DetailsCOMPLEX1_75K_3 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 3. RCIqCtRCIrF
ChainResidueDetails
AARG175-PHE185

site_idPS00644
Number of Residues16
DetailsCOMPLEX1_51K_1 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 1. GAGAYICGEETALIES
ChainResidueDetails
8GLY200-SER215

site_idPS00645
Number of Residues12
DetailsCOMPLEX1_51K_2 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 2. ESCGqCtPCReG
ChainResidueDetails
8GLU377-GLY388

site_idPS00667
Number of Residues16
DetailsCOMPLEX1_ND1_1 Respiratory-chain NADH dehydrogenase subunit 1 signature 1. GLLQpIaDAIKLFiKE
ChainResidueDetails
1GLY44-GLU59

site_idPS00668
Number of Residues14
DetailsCOMPLEX1_ND1_2 Respiratory-chain NADH dehydrogenase subunit 1 signature 2. PFDLTEGEseLVs.G
ChainResidueDetails
1PRO197-GLY210

site_idPS00848
Number of Residues23
DetailsCOX5B_1 Cytochrome c oxidase subunit Vb, zinc binding region signature. VIWfwlhkgeaqrCpsCGthYKL
ChainResidueDetails
A6VAL69-LEU91

site_idPS01099
Number of Residues19
DetailsCOMPLEX1_24K Respiratory-chain NADH dehydrogenase 24 Kd subunit signature. DklFTlieveCLGaCvnAP
ChainResidueDetails
9ASP166-PRO184

site_idPS01150
Number of Residues17
DetailsCOMPLEX1_20K Respiratory-chain NADH dehydrogenase 20 Kd subunit signature. GcDRIVPVDIYvPgCPP
ChainResidueDetails
DGLY172-PRO188

site_idPS01329
Number of Residues18
DetailsCOX6A Cytochrome c oxidase subunit VIa signature. IRtKpFsWGDGnHTfFhN
ChainResidueDetails
A4ILE55-ASN72

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27509854","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5LC5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LDX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9D6J6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"UniProtKB","id":"P19404","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1401
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsModified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"17060615","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"17060615","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3141400","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues57
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q91YT0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q91YT0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"Q91YT0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues78
DetailsDomain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues39
DetailsDomain: {"description":"4Fe-4S His(Cys)3-ligated-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01184","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues56
DetailsDomain: {"description":"4Fe-4S Mo/W bis-MGD-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01004","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q56223","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01184","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q91VD9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues7
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q91WD5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"Symmetric dimethylarginine","evidences":[{"source":"PubMed","id":"23836892","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues1
DetailsModified residue: {"description":"Hydroxyarginine","evidences":[{"source":"PubMed","id":"23836892","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues29
DetailsDomain: {"description":"4Fe-4S ferredoxin-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues29
DetailsDomain: {"description":"4Fe-4S ferredoxin-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P56181","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues121
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20433953","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI27
Number of Residues132
DetailsDomain: {"description":"CHCH","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI28
Number of Residues30
DetailsMotif: {"description":"Cx9C motif 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI29
Number of Residues30
DetailsMotif: {"description":"Cx9C motif 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI30
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9CQ75","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI31
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CQ75","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI32
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q16718","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI33
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CPP6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI34
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q63362","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI35
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9CPP6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI36
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9Z1P6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI37
Number of Residues41
DetailsDomain: {"description":"CHCH 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI38
Number of Residues43
DetailsDomain: {"description":"CHCH 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI39
Number of Residues10
DetailsMotif: {"description":"Cx9C motif 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI40
Number of Residues10
DetailsMotif: {"description":"Cx9C motif 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI41
Number of Residues13
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI42
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9DC69","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI43
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DC69","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI44
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q99LC3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI45
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PINK1","evidences":[{"source":"UniProtKB","id":"Q99LC3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI46
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"12381726","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17060615","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI47
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"9827566","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI48
Number of Residues150
DetailsDomain: {"description":"Carrier","evidences":[{"source":"PROSITE-ProRule","id":"PRU00258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI49
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CR21","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI50
Number of Residues2
DetailsModified residue: {"description":"O-(pantetheine 4'-phosphoryl)serine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00258","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1907568","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI51
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9CQZ6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI52
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O95168","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI53
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q3UIU2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI54
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9CR61","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI55
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9Y6M9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI56
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O96000","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI57
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P31930","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI58
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CZ13","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI59
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9CZ13","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI60
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q68FY0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI61
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DB77","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI62
Number of Residues322
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PDB","id":"1L0L","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI63
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00968","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12269811","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15312779","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16024040","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16924113","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9204897","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1L0L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1L0N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NU1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PP9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PPJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A06","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FYU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YBB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4D6T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4D6U","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI64
Number of Residues4
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"12269811","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15312779","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16024040","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16924113","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9204897","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BE3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BGY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1L0L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1L0N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PP9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PPJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A06","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FYU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YBB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4D6T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4D6U","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI65
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"12269811","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15312779","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16024040","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16924113","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9204897","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1L0N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NU1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PP9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PPJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A06","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FYU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YBB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4D6T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4D6U","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI66
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15312779","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16024040","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PP9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A06","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YBB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI67
Number of Residues418
DetailsTopological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI68
Number of Residues288
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI69
Number of Residues178
DetailsTopological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI70
Number of Residues202
DetailsDomain: {"description":"Cytochrome c","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI71
Number of Residues4
DetailsBinding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BE3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BGY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI72
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BE3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BGY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI73
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BE3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI74
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BE3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BGY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI75
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9D855","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI76
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9D855","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI77
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9CQ69","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI78
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P99028","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI79
Number of Residues75
DetailsTopological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"2165784","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI80
Number of Residues76
DetailsTransmembrane: {"description":"Helical; Name=I","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI81
Number of Residues9
DetailsTopological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8638158","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI82
Number of Residues87
DetailsTransmembrane: {"description":"Helical; Name=II","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI83
Number of Residues54
DetailsTransmembrane: {"description":"Helical; Name=III","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI84
Number of Residues47
DetailsTopological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"2165784","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI85
Number of Residues52
DetailsTransmembrane: {"description":"Helical; Name=IV","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI86
Number of Residues56
DetailsTransmembrane: {"description":"Helical; Name=V","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI87
Number of Residues65
DetailsTransmembrane: {"description":"Helical; Name=VI","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI88
Number of Residues39
DetailsTransmembrane: {"description":"Helical; Name=VII","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI89
Number of Residues28
DetailsTransmembrane: {"description":"Helical; Name=VIII","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI90
Number of Residues120
DetailsTopological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI91
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=IX","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI92
Number of Residues279
DetailsTopological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI93
Number of Residues29
DetailsTransmembrane: {"description":"Helical; Name=X","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI94
Number of Residues26
DetailsTransmembrane: {"description":"Helical; Name=XI","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI95
Number of Residues31
DetailsTransmembrane: {"description":"Helical; Name=XII","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI96
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23537388","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI97
Number of Residues3
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"20385840","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8638158","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI98
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20385840","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8638158","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI99
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI100
Number of Residues1
DetailsModified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"2165784","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI101
Number of Residues2
DetailsCross-link: {"description":"1'-histidyl-3'-tyrosine (His-Tyr)","evidences":[{"source":"PubMed","id":"10338009","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI102
Number of Residues1
DetailsModified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"220175","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI103
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P00406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI104
Number of Residues192
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI105
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P19783","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI106
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P13073","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI107
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P10888","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI108
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P19783","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI109
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P12787","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI110
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P20674","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI111
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20385840","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8638158","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI112
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P19536","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI113
Number of Residues10
DetailsMotif: {"description":"Cx9C motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI114
Number of Residues11
DetailsMotif: {"description":"Cx10C motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI115
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P56391","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI116
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P17665","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues14
DetailsM-CSA 124
ChainResidueDetails

246704

PDB entries from 2025-12-24

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