ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial

Intermolecular
Cysteine 727 of NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial and cysteine 112
Intramolecular
Cysteine 87 and cysteine 115
Cysteine 112 and cysteine 115
Cysteine 79 and cysteine 104
A redox-regulated disulphide may form between cysteine 727 of NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial and cysteine 112 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial (704 and 84 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
7qso
Structure name
bovine complex i in lipid nanodisc, state 3 (slack)
Structure deposition date
2022-01-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
nan
Peptide A name
NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
Peptide B name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
Peptide A accession
P15690
Peptide B accession
P23934
Peptide A residue number
727
Peptide B residue number
112

Ligandability

Cysteine 727 of NADH-ubiquinone oxidoreductase 75 kDa subunit, 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 112 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, 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 NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial between cysteines 87 and 115 (59 and 87 respectively in this structure).

Details

Redox score ?
71
PDB code
7qsd
Structure name
bovine complex i in the active state at 3
Structure deposition date
2022-01-13
Thiol separation (Å)
3
Half-sphere exposure sum ?
74
Minimum pKa ?
10
% buried
78
Peptide accession
P23934
Residue number A
87
Residue number B
115
Peptide name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial

Ligandability

Cysteine 87 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, 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 115 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, 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 NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial between cysteines 112 and 115 (84 and 87 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
7qsd
Structure name
bovine complex i in the active state at 3
Structure deposition date
2022-01-13
Thiol separation (Å)
3
Half-sphere exposure sum ?
76
Minimum pKa ?
19
% buried
nan
Peptide accession
P23934
Residue number A
112
Residue number B
115
Peptide name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial

Ligandability

Cysteine 112 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, 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 115 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, 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 NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial between cysteines 79 and 104 (59 and 84 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
6g2j
Structure name
mouse mitochondrial complex i in the active state
Structure deposition date
2018-03-23
Thiol separation (Å)
3
Half-sphere exposure sum ?
60
Minimum pKa ?
19
% buried
nan
Peptide accession
P52503
Residue number A
79
Residue number B
104
Peptide name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial

Ligandability

Cysteine 79 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, 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 104 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, 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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