ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Unconventional myosin-Ic

Intramolecular
Cysteine 437 and cysteine 441
A redox-regulated disulphide may form within Unconventional myosin-Ic between cysteines 437 and 441 (402 and 406 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
4byf
Structure name
crystal structure of human myosin 1c in complex with calmodulin in the pre-power stroke state
Structure deposition date
2013-07-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00159
Residue number A
437
Residue number B
441
Peptide name
Unconventional myosin-Ic

Ligandability

Cysteine 437 of Unconventional myosin-Ic

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 441 of Unconventional myosin-Ic

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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