ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Unconventional myosin-Vb

Intramolecular
Cysteine 1761 and cysteine 1764
Cysteine 1499 and cysteine 1554
Cysteine 1499 and cysteine 1559
A redox-regulated disulphide may form within Unconventional myosin-Vb between cysteines 1761 and 1764. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
4lx0
Structure name
crystal structure of myo5b globular tail domain in complex with active rab11a
Structure deposition date
2013-07-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
71
Peptide accession
Q9ULV0
Residue number A
1761
Residue number B
1764
Peptide name
Unconventional myosin-Vb

Ligandability

Cysteine 1761 of Unconventional myosin-Vb

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 1764 of Unconventional myosin-Vb

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-Vb between cysteines 1499 and 1554. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
4j5m
Structure name
structure of the cargo binding domain from human myosin vb
Structure deposition date
2013-02-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
11
% buried
100
Peptide accession
Q9ULV0
Residue number A
1499
Residue number B
1554
Peptide name
Unconventional myosin-Vb

Ligandability

Cysteine 1499 of Unconventional myosin-Vb

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 1554 of Unconventional myosin-Vb

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-Vb between cysteines 1499 and 1559. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
4lwz
Structure name
crystal structure of myo5b globular tail domain in complex with inactive rab11a
Structure deposition date
2013-07-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
89
Minimum pKa ?
11
% buried
100
Peptide accession
Q9ULV0
Residue number A
1499
Residue number B
1559
Peptide name
Unconventional myosin-Vb

Ligandability

Cysteine 1499 of Unconventional myosin-Vb

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 1559 of Unconventional myosin-Vb

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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