ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Intramolecular
Cysteine 561 and cysteine 589
Cysteine 589 and cysteine 592
Cysteine 561 and cysteine 592
Cysteine 561 and cysteine 586
Cysteine 586 and cysteine 589
Cysteine 586 and cysteine 592
Cysteine 248 and cysteine 387
Cysteine 248 and cysteine 589
A redox-regulated disulphide may form within Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial between cysteines 561 and 589 (528 and 556 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
2gmh
Structure name
structure of porcine electron transfer flavoprotein-ubiquinone oxidoreductase in complexed with ubiquinone
Structure deposition date
2006-04-06
Thiol separation (Å)
6
Half-sphere exposure sum ?
86
Minimum pKa ?
11
% buried
100
Peptide accession
P55931
Residue number A
561
Residue number B
589
Peptide name
Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Ligandability

Cysteine 561 of Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 589 of Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial between cysteines 589 and 592 (556 and 559 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
2gmh
Structure name
structure of porcine electron transfer flavoprotein-ubiquinone oxidoreductase in complexed with ubiquinone
Structure deposition date
2006-04-06
Thiol separation (Å)
6
Half-sphere exposure sum ?
87
Minimum pKa ?
11
% buried
100
Peptide accession
P55931
Residue number A
589
Residue number B
592
Peptide name
Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Ligandability

Cysteine 589 of Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 592 of Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial between cysteines 561 and 592 (528 and 559 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
2gmh
Structure name
structure of porcine electron transfer flavoprotein-ubiquinone oxidoreductase in complexed with ubiquinone
Structure deposition date
2006-04-06
Thiol separation (Å)
6
Half-sphere exposure sum ?
88
Minimum pKa ?
13
% buried
100
Peptide accession
P55931
Residue number A
561
Residue number B
592
Peptide name
Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Ligandability

Cysteine 561 of Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 592 of Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial between cysteines 561 and 586 (528 and 553 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
2gmh
Structure name
structure of porcine electron transfer flavoprotein-ubiquinone oxidoreductase in complexed with ubiquinone
Structure deposition date
2006-04-06
Thiol separation (Å)
7
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
100
Peptide accession
P55931
Residue number A
561
Residue number B
586
Peptide name
Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Ligandability

Cysteine 561 of Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 586 of Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial between cysteines 586 and 589 (553 and 556 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
2gmj
Structure name
structure of porcine electron transfer flavoprotein- ubiquinone oxidoreductase
Structure deposition date
2006-04-06
Thiol separation (Å)
7
Half-sphere exposure sum ?
85
Minimum pKa ?
11
% buried
100
Peptide accession
P55931
Residue number A
586
Residue number B
589
Peptide name
Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Ligandability

Cysteine 586 of Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 589 of Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial between cysteines 586 and 592 (553 and 559 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
2gmj
Structure name
structure of porcine electron transfer flavoprotein- ubiquinone oxidoreductase
Structure deposition date
2006-04-06
Thiol separation (Å)
7
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
100
Peptide accession
P55931
Residue number A
586
Residue number B
592
Peptide name
Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Ligandability

Cysteine 586 of Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 592 of Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial between cysteines 248 and 387 (215 and 354 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
2gmj
Structure name
structure of porcine electron transfer flavoprotein- ubiquinone oxidoreductase
Structure deposition date
2006-04-06
Thiol separation (Å)
6
Half-sphere exposure sum ?
91
Minimum pKa ?
13
% buried
100
Peptide accession
P55931
Residue number A
248
Residue number B
387
Peptide name
Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Ligandability

Cysteine 248 of Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 387 of Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial between cysteines 248 and 589 (215 and 556 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
2gmh
Structure name
structure of porcine electron transfer flavoprotein-ubiquinone oxidoreductase in complexed with ubiquinone
Structure deposition date
2006-04-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
91
Minimum pKa ?
11
% buried
100
Peptide accession
P55931
Residue number A
248
Residue number B
589
Peptide name
Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Ligandability

Cysteine 248 of Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 589 of Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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