ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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LIM domain kinase 1

Intramolecular
Cysteine 571 and cysteine 575 L
Cysteine 540 and cysteine 587
Cysteine 586 and cysteine 587
Cysteine 540 and cysteine 571 L
Cysteine 540 and cysteine 586
A redox-regulated disulphide may form within LIM domain kinase 1 between cysteines 571 and 575.

Details

Redox score ?
75
PDB code
5hvj
Structure name
crystal structure of limk1 d460n mutant in complex with amp-pnp
Structure deposition date
2016-01-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
78
Peptide accession
P53667
Residue number A
571
Residue number B
575
Peptide name
LIM domain kinase 1

Ligandability

Cysteine 571 of LIM domain kinase 1

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.

Cysteine 575 of LIM domain kinase 1

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 LIM domain kinase 1 between cysteines 540 and 587.

Details

Redox score ?
65
PDB code
5hvj
Structure name
crystal structure of limk1 d460n mutant in complex with amp-pnp
Structure deposition date
2016-01-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
90
Minimum pKa ?
8
% buried
100
Peptide accession
P53667
Residue number A
540
Residue number B
587
Peptide name
LIM domain kinase 1

Ligandability

Cysteine 540 of LIM domain kinase 1

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 587 of LIM domain kinase 1

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 LIM domain kinase 1 between cysteines 586 and 587. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
7atu
Structure name
the limk1 kinase domain bound to lijtf500025
Structure deposition date
2020-10-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
81
Minimum pKa ?
9
% buried
100
Peptide accession
P53667
Residue number A
586
Residue number B
587
Peptide name
LIM domain kinase 1

Ligandability

Cysteine 586 of LIM domain kinase 1

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 587 of LIM domain kinase 1

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 LIM domain kinase 1 between cysteines 540 and 571. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
7atu
Structure name
the limk1 kinase domain bound to lijtf500025
Structure deposition date
2020-10-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
7
% buried
74
Peptide accession
P53667
Residue number A
540
Residue number B
571
Peptide name
LIM domain kinase 1

Ligandability

Cysteine 540 of LIM domain kinase 1

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 571 of LIM domain kinase 1

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 LIM domain kinase 1 between cysteines 540 and 586. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
7b8w
Structure name
structure of limk1 kinase domain with allosteric inhibitor th-470
Structure deposition date
2020-12-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
88
Minimum pKa ?
14
% buried
100
Peptide accession
P53667
Residue number A
540
Residue number B
586
Peptide name
LIM domain kinase 1

Ligandability

Cysteine 540 of LIM domain kinase 1

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 586 of LIM domain kinase 1

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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