ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Serine/threonine-protein kinase TBK1

Intermolecular
Cysteine 91 and cysteine 558
Intramolecular
Cysteine 423 and cysteine 426 L
Cysteine 89 and cysteine 91
Cysteine 426 and cysteine 605 L
A redox-regulated disulphide may form between two units of Serine/threonine-protein kinase TBK1 at cysteines 91 and 558. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
6o8b
Structure name
crystal structure of sting ctd in complex with tbk1
Structure deposition date
2019-03-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
51
Minimum pKa ?
10
% buried
48
Peptide A name
Serine/threonine-protein kinase TBK1
Peptide B name
Serine/threonine-protein kinase TBK1
Peptide A accession
Q9UHD2
Peptide B accession
Q9UHD2
Peptide A residue number
91
Peptide B residue number
558

Ligandability

Cysteine 91 of Serine/threonine-protein kinase TBK1

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 558 of Serine/threonine-protein kinase TBK1

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 Serine/threonine-protein kinase TBK1 between cysteines 423 and 426. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
6bny
Structure name
tbk1 in complex with tetrazole analog of amlexanox
Structure deposition date
2017-11-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
75
Minimum pKa ?
10
% buried
73
Peptide accession
Q9UHD2
Residue number A
423
Residue number B
426
Peptide name
Serine/threonine-protein kinase TBK1

Ligandability

Cysteine 423 of Serine/threonine-protein kinase TBK1

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 426 of Serine/threonine-protein kinase TBK1

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 Serine/threonine-protein kinase TBK1 between cysteines 89 and 91. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
4jl9
Structure name
crystal structure of mouse tbk1 bound to bx795
Structure deposition date
2013-03-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
9
% buried
48
Peptide accession
Q9WUN2
Residue number A
89
Residue number B
91
Peptide name
Serine/threonine-protein kinase TBK1

Ligandability

Cysteine 89 of Serine/threonine-protein kinase TBK1

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 91 of Serine/threonine-protein kinase TBK1

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 Serine/threonine-protein kinase TBK1 between cysteines 426 and 605. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
6o8b
Structure name
crystal structure of sting ctd in complex with tbk1
Structure deposition date
2019-03-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
11
% buried
76
Peptide accession
Q9UHD2
Residue number A
426
Residue number B
605
Peptide name
Serine/threonine-protein kinase TBK1

Ligandability

Cysteine 426 of Serine/threonine-protein kinase TBK1

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 605 of Serine/threonine-protein kinase TBK1

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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