ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Kinesin light chain

Intramolecular
Cysteine 441 and cysteine 474
Cysteine 305 and cysteine 334
Cysteine 334 and cysteine 375
A redox-regulated disulphide may form within Kinesin light chain between cysteines 441 and 474.

Details

Redox score ?
85
PDB code
5fjy
Structure name
crystal structure of mouse kinesin light chain 2 (residues 161-480)
Structure deposition date
2015-10-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91YS4
Residue number A
441
Residue number B
474
Peptide name
Kinesin light chain

Ligandability

Cysteine 441 of Kinesin light chain

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 474 of Kinesin light chain

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 light chain between cysteines 305 and 334. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
5fjy
Structure name
crystal structure of mouse kinesin light chain 2 (residues 161-480)
Structure deposition date
2015-10-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
10
% buried
62
Peptide accession
Q91YS4
Residue number A
305
Residue number B
334
Peptide name
Kinesin light chain

Ligandability

Cysteine 305 of Kinesin light chain

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 334 of Kinesin light chain

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 light chain between cysteines 334 and 375. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
5fjy
Structure name
crystal structure of mouse kinesin light chain 2 (residues 161-480)
Structure deposition date
2015-10-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
47
Peptide accession
Q91YS4
Residue number A
334
Residue number B
375
Peptide name
Kinesin light chain

Ligandability

Cysteine 334 of Kinesin light chain

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 375 of Kinesin light chain

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.

If this tool was useful for finding a disulphide, please cite: