ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Dual specificity protein kinase CLK3

Intramolecular
Cysteine 294 and cysteine 321
Cysteine 294 and cysteine 381
Cysteine 321 and cysteine 381
Cysteine 503 and cysteine 510
A redox-regulated disulphide may form within Dual specificity protein kinase CLK3 between cysteines 294 and 321 (146 and 173 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
6ft7
Structure name
crystal structure of clk3 in complex with compound 8a
Structure deposition date
2018-02-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
71
Peptide accession
P49761
Residue number A
294
Residue number B
321
Peptide name
Dual specificity protein kinase CLK3

Ligandability

Cysteine 294 of Dual specificity protein kinase CLK3

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 321 of Dual specificity protein kinase CLK3

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 Dual specificity protein kinase CLK3 between cysteines 294 and 381 (146 and 233 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
6fyr
Structure name
x-ray structure of clk3-kd(gp-[275-632], non-phos
Structure deposition date
2018-03-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
80
Peptide accession
P49761
Residue number A
294
Residue number B
381
Peptide name
Dual specificity protein kinase CLK3

Ligandability

Cysteine 294 of Dual specificity protein kinase CLK3

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 381 of Dual specificity protein kinase CLK3

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 Dual specificity protein kinase CLK3 between cysteines 321 and 381 (173 and 233 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
3raw
Structure name
crystal structure of human cdc-like kinase 3 isoform in complex with leucettine l41
Structure deposition date
2011-03-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
84
Peptide accession
P49761
Residue number A
321
Residue number B
381
Peptide name
Dual specificity protein kinase CLK3

Ligandability

Cysteine 321 of Dual specificity protein kinase CLK3

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 381 of Dual specificity protein kinase CLK3

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 Dual specificity protein kinase CLK3 between cysteines 503 and 510 (355 and 362 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
21
PDB code
3raw
Structure name
crystal structure of human cdc-like kinase 3 isoform in complex with leucettine l41
Structure deposition date
2011-03-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
88
Minimum pKa ?
13
% buried
100
Peptide accession
P49761
Residue number A
503
Residue number B
510
Peptide name
Dual specificity protein kinase CLK3

Ligandability

Cysteine 503 of Dual specificity protein kinase CLK3

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 510 of Dual specificity protein kinase CLK3

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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