ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Kinesin-like protein

Intramolecular
Cysteine 13 and cysteine 302
Cysteine 301 and cysteine 302
Cysteine 13 and cysteine 301
A redox-regulated disulphide may form within Kinesin-like protein between cysteines 13 and 302.

Details

Redox score ?
61
PDB code
5lt2
Structure name
nucleotide-free kinesin-1 motor domain, p1 crystal form
Structure deposition date
2016-09-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
96
Minimum pKa ?
9
% buried
98
Peptide accession
Q6P164
Residue number A
13
Residue number B
302
Peptide name
Kinesin-like protein

Ligandability

Cysteine 13 of Kinesin-like protein

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 302 of Kinesin-like protein

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 Kinesin-like protein between cysteines 301 and 302. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
5lt2
Structure name
nucleotide-free kinesin-1 motor domain, p1 crystal form
Structure deposition date
2016-09-06
Thiol separation (Å)
7
Half-sphere exposure sum ?
92
Minimum pKa ?
9
% buried
96
Peptide accession
Q6P164
Residue number A
301
Residue number B
302
Peptide name
Kinesin-like protein

Ligandability

Cysteine 301 of Kinesin-like protein

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 302 of Kinesin-like protein

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 Kinesin-like protein between cysteines 13 and 301. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
5lt2
Structure name
nucleotide-free kinesin-1 motor domain, p1 crystal form
Structure deposition date
2016-09-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
91
Minimum pKa ?
11
% buried
100
Peptide accession
Q6P164
Residue number A
13
Residue number B
301
Peptide name
Kinesin-like protein

Ligandability

Cysteine 13 of Kinesin-like protein

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 301 of Kinesin-like protein

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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