ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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2-oxoadipate dehydrogenase complex component E1

Intramolecular
Cysteine 720 and cysteine 839
Cysteine 337 and cysteine 383 L
Cysteine 383 and cysteine 429 L
A redox-regulated disulphide may form within 2-oxoadipate dehydrogenase complex component E1 between cysteines 720 and 839 (699 and 818 respectively in this structure).

Details

Redox score ?
67
PDB code
5rw1
Structure name
pandda analysis group deposition of ground-state model of dhtkd1
Structure deposition date
2020-10-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
88
Minimum pKa ?
10
% buried
100
Peptide accession
Q96HY7
Residue number A
720
Residue number B
839
Peptide name
2-oxoadipate dehydrogenase complex component E1

Ligandability

Cysteine 720 of 2-oxoadipate 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 839 of 2-oxoadipate 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-oxoadipate dehydrogenase complex component E1 between cysteines 337 and 383. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
6u3j
Structure name
structure of the 2-oxoadipate dehydrogenase dhtkd1
Structure deposition date
2019-08-21
Thiol separation (Å)
5
Half-sphere exposure sum ?
92
Minimum pKa ?
13
% buried
100
Peptide accession
Q96HY7
Residue number A
337
Residue number B
383
Peptide name
2-oxoadipate dehydrogenase complex component E1

Ligandability

Cysteine 337 of 2-oxoadipate 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 383 of 2-oxoadipate dehydrogenase complex component E1

Not ligandable in the dataset of Yang et al.

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-oxoadipate dehydrogenase complex component E1 between cysteines 383 and 429. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
5rvy
Structure name
pandda analysis group deposition -- crystal structure of dhtkd1 in complex with z437516460
Structure deposition date
2020-10-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
87
Minimum pKa ?
13
% buried
100
Peptide accession
Q96HY7
Residue number A
383
Residue number B
429
Peptide name
2-oxoadipate dehydrogenase complex component E1

Ligandability

Cysteine 383 of 2-oxoadipate dehydrogenase complex component E1

Not ligandable in the dataset of Yang et al.

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 429 of 2-oxoadipate 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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