ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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2-oxoglutarate dehydrogenase complex component E1

Intramolecular
Cysteine 283 and cysteine 507 L
Cysteine 904 and cysteine 956
Cysteine 802 and cysteine 825
Cysteine 763 and cysteine 802
A redox-regulated disulphide may form within 2-oxoglutarate dehydrogenase complex component E1 between cysteines 283 and 507.

Details

Redox score ?
71
PDB code
7wgr
Structure name
cryo-electron microscopic structure of the 2-oxoglutarate dehydrogenase (e1) component of the human alpha-ketoglutarate (2- oxoglutarate) dehydrogenase complex
Structure deposition date
2021-12-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
8
% buried
100
Peptide accession
Q02218
Residue number A
283
Residue number B
507
Peptide name
2-oxoglutarate dehydrogenase complex component E1

Ligandability

Cysteine 283 of 2-oxoglutarate dehydrogenase complex component E1

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 507 of 2-oxoglutarate dehydrogenase complex component E1

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 2-oxoglutarate dehydrogenase complex component E1 between cysteines 904 and 956. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
7wgr
Structure name
cryo-electron microscopic structure of the 2-oxoglutarate dehydrogenase (e1) component of the human alpha-ketoglutarate (2- oxoglutarate) dehydrogenase complex
Structure deposition date
2021-12-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
85
Minimum pKa ?
12
% buried
100
Peptide accession
Q02218
Residue number A
904
Residue number B
956
Peptide name
2-oxoglutarate dehydrogenase complex component E1

Ligandability

Cysteine 904 of 2-oxoglutarate dehydrogenase complex component E1

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 956 of 2-oxoglutarate dehydrogenase complex component E1

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 2-oxoglutarate dehydrogenase complex component E1 between cysteines 802 and 825. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
7wgr
Structure name
cryo-electron microscopic structure of the 2-oxoglutarate dehydrogenase (e1) component of the human alpha-ketoglutarate (2- oxoglutarate) dehydrogenase complex
Structure deposition date
2021-12-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
94
Peptide accession
Q02218
Residue number A
802
Residue number B
825
Peptide name
2-oxoglutarate dehydrogenase complex component E1

Ligandability

Cysteine 802 of 2-oxoglutarate dehydrogenase complex component E1

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 825 of 2-oxoglutarate dehydrogenase complex component E1

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 2-oxoglutarate dehydrogenase complex component E1 between cysteines 763 and 802. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
7wgr
Structure name
cryo-electron microscopic structure of the 2-oxoglutarate dehydrogenase (e1) component of the human alpha-ketoglutarate (2- oxoglutarate) dehydrogenase complex
Structure deposition date
2021-12-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
100
Peptide accession
Q02218
Residue number A
763
Residue number B
802
Peptide name
2-oxoglutarate dehydrogenase complex component E1

Ligandability

Cysteine 763 of 2-oxoglutarate dehydrogenase complex component E1

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 802 of 2-oxoglutarate dehydrogenase complex component E1

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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