ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Unconventional myosin-X

Intramolecular
Cysteine 140 and cysteine 143
Cysteine 1706 and cysteine 1712
Cysteine 1634 and cysteine 1637
Cysteine 408 and cysteine 409
Cysteine 140 and cysteine 152
A redox-regulated disulphide may form within Unconventional myosin-X between cysteines 140 and 143. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
5i0i
Structure name
crystal structure of myosin x motor domain with 2iq motifs in pre- powerstroke state
Structure deposition date
2016-02-04
Thiol separation (Å)
7
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9HD67
Residue number A
140
Residue number B
143
Peptide name
Unconventional myosin-X

Ligandability

Cysteine 140 of Unconventional myosin-X

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 143 of Unconventional myosin-X

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-X between cysteines 1706 and 1712. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
3au5
Structure name
structure of the human myosin-x myth4-ferm cassette
Structure deposition date
2011-01-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
32
Peptide accession
Q9HD67
Residue number A
1706
Residue number B
1712
Peptide name
Unconventional myosin-X

Ligandability

Cysteine 1706 of Unconventional myosin-X

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 1712 of Unconventional myosin-X

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-X between cysteines 1634 and 1637. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3au4
Structure name
structure of the human myosin-x myth4-ferm cassette bound to its specific cargo, dcc
Structure deposition date
2011-01-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
91
Minimum pKa ?
11
% buried
100
Peptide accession
Q9HD67
Residue number A
1634
Residue number B
1637
Peptide name
Unconventional myosin-X

Ligandability

Cysteine 1634 of Unconventional myosin-X

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 1637 of Unconventional myosin-X

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-X between cysteines 408 and 409. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
5i0i
Structure name
crystal structure of myosin x motor domain with 2iq motifs in pre- powerstroke state
Structure deposition date
2016-02-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9HD67
Residue number A
408
Residue number B
409
Peptide name
Unconventional myosin-X

Ligandability

Cysteine 408 of Unconventional myosin-X

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 409 of Unconventional myosin-X

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-X between cysteines 140 and 152. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5i0h
Structure name
crystal structure of myosin x motor domain in pre-powerstroke state
Structure deposition date
2016-02-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
100
Peptide accession
Q9HD67
Residue number A
140
Residue number B
152
Peptide name
Unconventional myosin-X

Ligandability

Cysteine 140 of Unconventional myosin-X

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 152 of Unconventional myosin-X

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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