ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Mitochondrial potassium channel ATP-binding subunit

Intramolecular
Cysteine 461 and cysteine 462
Cysteine 323 and cysteine 364
Cysteine 364 and cysteine 366
A redox-regulated disulphide may form within Mitochondrial potassium channel ATP-binding subunit between cysteines 461 and 462.

Details

Redox score ?
65
PDB code
5och
Structure name
the crystal structure of human abcb8 in an outward-facing state
Structure deposition date
2017-06-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
45
Minimum pKa ?
8
% buried
0
Peptide accession
Q9NUT2
Residue number A
461
Residue number B
462
Peptide name
Mitochondrial potassium channel ATP-binding subunit

Ligandability

Cysteine 461 of Mitochondrial potassium channel ATP-binding subunit

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 462 of Mitochondrial potassium channel ATP-binding subunit

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 Mitochondrial potassium channel ATP-binding subunit between cysteines 323 and 364. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
5och
Structure name
the crystal structure of human abcb8 in an outward-facing state
Structure deposition date
2017-06-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
82
Peptide accession
Q9NUT2
Residue number A
323
Residue number B
364
Peptide name
Mitochondrial potassium channel ATP-binding subunit

Ligandability

Cysteine 323 of Mitochondrial potassium channel ATP-binding subunit

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 364 of Mitochondrial potassium channel ATP-binding subunit

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 Mitochondrial potassium channel ATP-binding subunit between cysteines 364 and 366. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7ehl
Structure name
cryo-em structure of human abcb8 transporter in nucleotide binding state
Structure deposition date
2021-03-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
50
Minimum pKa ?
9
% buried
24
Peptide accession
Q9NUT2
Residue number A
364
Residue number B
366
Peptide name
Mitochondrial potassium channel ATP-binding subunit

Ligandability

Cysteine 364 of Mitochondrial potassium channel ATP-binding subunit

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 366 of Mitochondrial potassium channel ATP-binding subunit

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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