ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Dihydrolipoyl dehydrogenase, mitochondrial

Intermolecular
Cysteine 484 and cysteine 388 L
Intramolecular
Cysteine 80 and cysteine 85 L
Cysteine 9 and cysteine 312 L
A redox-regulated disulphide may form between two units of Dihydrolipoyl dehydrogenase, mitochondrial at cysteines 484 and 388 (449 and 353 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
1zmd
Structure name
crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh
Structure deposition date
2005-05-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
13
% buried
82
Peptide A name
Dihydrolipoyl dehydrogenase, mitochondrial
Peptide B name
Dihydrolipoyl dehydrogenase, mitochondrial
Peptide A accession
P09622
Peptide B accession
P09622
Peptide A residue number
484
Peptide B residue number
388

Ligandability

Cysteine 484 of Dihydrolipoyl dehydrogenase, 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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 388 of Dihydrolipoyl dehydrogenase, 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 Dihydrolipoyl dehydrogenase, mitochondrial between cysteines 80 and 85 (45 and 50 respectively in this structure).

Details

Redox score ?
73
PDB code
6i4r
Structure name
crystal structure of the disease-causing r460g mutant of the human dihydrolipoamide dehydrogenase at 1
Structure deposition date
2018-11-10
Thiol separation (Å)
3
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
50
Peptide accession
P09622
Residue number A
80
Residue number B
85
Peptide name
Dihydrolipoyl dehydrogenase, mitochondrial

Ligandability

Cysteine 80 of Dihydrolipoyl dehydrogenase, 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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 85 of Dihydrolipoyl dehydrogenase, 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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dihydrolipoyl dehydrogenase, mitochondrial between cysteines 9 and 312 (194 and 277 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
6i4p
Structure name
crystal structure of the disease-causing g194c mutant of the human dihydrolipoamide dehydrogenase
Structure deposition date
2018-11-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
90
Minimum pKa ?
13
% buried
100
Peptide accession
P09622
Residue number A
9
Residue number B
312
Peptide name
Dihydrolipoyl dehydrogenase, mitochondrial

Ligandability

Cysteine 9 of Dihydrolipoyl dehydrogenase, 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 312 of Dihydrolipoyl dehydrogenase, 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.

Ligandable in the dataset of Kuljanin et al.

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