ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

Intramolecular
Cysteine 41 and cysteine 261
Cysteine 94 and cysteine 101
Cysteine 190 and cysteine 218
Cysteine 181 and cysteine 190
Cysteine 218 and cysteine 273
Cysteine 100 and cysteine 101
Cysteine 181 and cysteine 218
Cysteine 181 and cysteine 273
Cysteine 94 and cysteine 100
Cysteine 190 and cysteine 273
More...
Cysteine 91 and cysteine 94
Cysteine 100 and cysteine 261
A redox-regulated disulphide may form within Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial between cysteines 41 and 261 (12 and 232 respectively in this structure).

Details

Redox score ?
71
PDB code
6cer
Structure name
human pyruvate dehydrogenase complex e1 component v138m mutation
Structure deposition date
2018-02-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
8
% buried
71
Peptide accession
P08559
Residue number A
41
Residue number B
261
Peptide name
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

Ligandability

Cysteine 41 of Pyruvate dehydrogenase E1 component subunit alpha, somatic form, 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 261 of Pyruvate dehydrogenase E1 component subunit alpha, somatic form, 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 Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial between cysteines 94 and 101 (65 and 72 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
3exg
Structure name
crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex
Structure deposition date
2008-10-16
Thiol separation (Å)
5
Half-sphere exposure sum ?
85
Minimum pKa ?
10
% buried
100
Peptide accession
P08559
Residue number A
94
Residue number B
101
Peptide name
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

Ligandability

Cysteine 94 of Pyruvate dehydrogenase E1 component subunit alpha, somatic form, 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 101 of Pyruvate dehydrogenase E1 component subunit alpha, somatic form, 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 Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial between cysteines 190 and 218 (161 and 189 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
3exf
Structure name
crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex
Structure deposition date
2008-10-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
104
Minimum pKa ?
12
% buried
100
Peptide accession
P08559
Residue number A
190
Residue number B
218
Peptide name
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

Ligandability

Cysteine 190 of Pyruvate dehydrogenase E1 component subunit alpha, somatic form, 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 218 of Pyruvate dehydrogenase E1 component subunit alpha, somatic form, 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 Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial between cysteines 181 and 190 (152 and 161 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
3exg
Structure name
crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex
Structure deposition date
2008-10-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
90
Minimum pKa ?
13
% buried
94
Peptide accession
P08559
Residue number A
181
Residue number B
190
Peptide name
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

Ligandability

Cysteine 181 of Pyruvate dehydrogenase E1 component subunit alpha, somatic form, 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 190 of Pyruvate dehydrogenase E1 component subunit alpha, somatic form, 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 Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial between cysteines 218 and 273 (189 and 244 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
3exf
Structure name
crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex
Structure deposition date
2008-10-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
90
Minimum pKa ?
13
% buried
100
Peptide accession
P08559
Residue number A
218
Residue number B
273
Peptide name
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

Ligandability

Cysteine 218 of Pyruvate dehydrogenase E1 component subunit alpha, somatic form, 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 273 of Pyruvate dehydrogenase E1 component subunit alpha, somatic form, 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 Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial between cysteines 100 and 101 (71 and 72 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
3exg
Structure name
crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex
Structure deposition date
2008-10-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
99
Minimum pKa ?
10
% buried
100
Peptide accession
P08559
Residue number A
100
Residue number B
101
Peptide name
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

Ligandability

Cysteine 100 of Pyruvate dehydrogenase E1 component subunit alpha, somatic form, 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 101 of Pyruvate dehydrogenase E1 component subunit alpha, somatic form, 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 Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial between cysteines 181 and 218 (152 and 189 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
3exg
Structure name
crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex
Structure deposition date
2008-10-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
93
Minimum pKa ?
12
% buried
94
Peptide accession
P08559
Residue number A
181
Residue number B
218
Peptide name
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

Ligandability

Cysteine 181 of Pyruvate dehydrogenase E1 component subunit alpha, somatic form, 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 218 of Pyruvate dehydrogenase E1 component subunit alpha, somatic form, 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 Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial between cysteines 181 and 273 (152 and 244 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
3exg
Structure name
crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex
Structure deposition date
2008-10-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
91
Peptide accession
P08559
Residue number A
181
Residue number B
273
Peptide name
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

Ligandability

Cysteine 181 of Pyruvate dehydrogenase E1 component subunit alpha, somatic form, 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 273 of Pyruvate dehydrogenase E1 component subunit alpha, somatic form, 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 Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial between cysteines 94 and 100 (65 and 71 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
6cer
Structure name
human pyruvate dehydrogenase complex e1 component v138m mutation
Structure deposition date
2018-02-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
14
% buried
100
Peptide accession
P08559
Residue number A
94
Residue number B
100
Peptide name
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

Ligandability

Cysteine 94 of Pyruvate dehydrogenase E1 component subunit alpha, somatic form, 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 100 of Pyruvate dehydrogenase E1 component subunit alpha, somatic form, 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 Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial between cysteines 190 and 273 (161 and 244 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
3exf
Structure name
crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex
Structure deposition date
2008-10-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
88
Minimum pKa ?
12
% buried
100
Peptide accession
P08559
Residue number A
190
Residue number B
273
Peptide name
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

Ligandability

Cysteine 190 of Pyruvate dehydrogenase E1 component subunit alpha, somatic form, 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 273 of Pyruvate dehydrogenase E1 component subunit alpha, somatic form, 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 Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial between cysteines 91 and 94 (62 and 65 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
3exf
Structure name
crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex
Structure deposition date
2008-10-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
85
Minimum pKa ?
13
% buried
100
Peptide accession
P08559
Residue number A
91
Residue number B
94
Peptide name
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

Ligandability

Cysteine 91 of Pyruvate dehydrogenase E1 component subunit alpha, somatic form, 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 94 of Pyruvate dehydrogenase E1 component subunit alpha, somatic form, 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 Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial between cysteines 100 and 261 (71 and 232 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
23
PDB code
3exg
Structure name
crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex
Structure deposition date
2008-10-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
92
Minimum pKa ?
13
% buried
91
Peptide accession
P08559
Residue number A
100
Residue number B
261
Peptide name
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

Ligandability

Cysteine 100 of Pyruvate dehydrogenase E1 component subunit alpha, somatic form, 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 261 of Pyruvate dehydrogenase E1 component subunit alpha, somatic form, 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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