ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Unconventional myosin-VI

Intramolecular
Cysteine 473 and cysteine 477
A redox-regulated disulphide may form within Unconventional myosin-VI between cysteines 473 and 477 (472 and 476 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
2v26
Structure name
myosin vi (md) pre-powerstroke state (mg
Structure deposition date
2007-06-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q29122
Residue number A
473
Residue number B
477
Peptide name
Unconventional myosin-VI

Ligandability

Cysteine 473 of Unconventional myosin-VI

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 477 of Unconventional myosin-VI

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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