ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Unconventional myosin-XV

Intramolecular
Cysteine 1294 and cysteine 1772
Cysteine 1649 and cysteine 1650
Cysteine 1831 and cysteine 1854
A redox-regulated disulphide may form within Unconventional myosin-XV between cysteines 1294 and 1772.

Details

Redox score ?
78
PDB code
7udt
Structure name
cryo-em structure of the rigor state wild type myosin-15-f-actin complex (symmetry expansion and re-centering)
Structure deposition date
2022-03-20
Thiol separation (Å)
3
Half-sphere exposure sum ?
64
Minimum pKa ?
7
% buried
80
Peptide accession
Q9QZZ4
Residue number A
1294
Residue number B
1772
Peptide name
Unconventional myosin-XV

Ligandability

Cysteine 1294 of Unconventional myosin-XV

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 1772 of Unconventional myosin-XV

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 Unconventional myosin-XV between cysteines 1649 and 1650. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
7udt
Structure name
cryo-em structure of the rigor state wild type myosin-15-f-actin complex (symmetry expansion and re-centering)
Structure deposition date
2022-03-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
98
Peptide accession
Q9QZZ4
Residue number A
1649
Residue number B
1650
Peptide name
Unconventional myosin-XV

Ligandability

Cysteine 1649 of Unconventional myosin-XV

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 1650 of Unconventional myosin-XV

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 Unconventional myosin-XV between cysteines 1831 and 1854. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
7udt
Structure name
cryo-em structure of the rigor state wild type myosin-15-f-actin complex (symmetry expansion and re-centering)
Structure deposition date
2022-03-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
40
Peptide accession
Q9QZZ4
Residue number A
1831
Residue number B
1854
Peptide name
Unconventional myosin-XV

Ligandability

Cysteine 1831 of Unconventional myosin-XV

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 1854 of Unconventional myosin-XV

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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