ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Proteasome 26S subunit, ATPase 6

Intramolecular
Cysteine 207 and cysteine 242
A redox-regulated disulphide may form within Proteasome 26S subunit, ATPase 6 between cysteines 207 and 242 (193 and 228 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
5t0g
Structure name
structural basis for dynamic regulation of the human 26s proteasome
Structure deposition date
2016-08-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
56
Minimum pKa ?
10
% buried
48
Peptide accession
A0A087X2I1
Residue number A
207
Residue number B
242
Peptide name
Proteasome 26S subunit, ATPase 6

Ligandability

Cysteine 207 of Proteasome 26S subunit, ATPase 6

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 242 of Proteasome 26S subunit, ATPase 6

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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