ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Kinesin-like protein KIF15

Intramolecular
Cysteine 50 and cysteine 346 L
Cysteine 294 and cysteine 314
Cysteine 162 and cysteine 164
A redox-regulated disulphide may form within Kinesin-like protein KIF15 between cysteines 50 and 346 (36 and 332 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
4bn2
Structure name
the crystal structure of kinesin-like protein kif15
Structure deposition date
2013-05-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
36
Peptide accession
Q9NS87
Residue number A
50
Residue number B
346
Peptide name
Kinesin-like protein KIF15

Ligandability

Cysteine 50 of Kinesin-like protein KIF15

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 346 of Kinesin-like protein KIF15

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Kinesin-like protein KIF15 between cysteines 294 and 314 (280 and 300 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
4bn2
Structure name
the crystal structure of kinesin-like protein kif15
Structure deposition date
2013-05-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
52
Minimum pKa ?
10
% buried
14
Peptide accession
Q9NS87
Residue number A
294
Residue number B
314
Peptide name
Kinesin-like protein KIF15

Ligandability

Cysteine 294 of Kinesin-like protein KIF15

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 314 of Kinesin-like protein KIF15

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 KIF15 between cysteines 162 and 164 (148 and 150 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
4bn2
Structure name
the crystal structure of kinesin-like protein kif15
Structure deposition date
2013-05-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
84
Peptide accession
Q9NS87
Residue number A
162
Residue number B
164
Peptide name
Kinesin-like protein KIF15

Ligandability

Cysteine 162 of Kinesin-like protein KIF15

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 164 of Kinesin-like protein KIF15

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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