ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Intraflagellar transport protein 140 homolog

Intramolecular
Cysteine 811 and cysteine 823
Cysteine 1198 and cysteine 1199 L
Cysteine 1159 and cysteine 1198 L
Cysteine 530 and cysteine 577
Cysteine 557 and cysteine 559
Cysteine 1159 and cysteine 1199 L
Cysteine 331 and cysteine 333
Cysteine 68 and cysteine 155
Cysteine 329 and cysteine 331
A redox-regulated disulphide may form within Intraflagellar transport protein 140 homolog between cysteines 811 and 823.

Details

Redox score ?
68
PDB code
8bbf
Structure name
structure of the ift-a complex; ift-a1 module
Structure deposition date
2022-10-12
Thiol separation (Å)
5
Half-sphere exposure sum ?
71
Minimum pKa ?
8
% buried
80
Peptide accession
Q96RY7
Residue number A
811
Residue number B
823
Peptide name
Intraflagellar transport protein 140 homolog

Ligandability

Cysteine 811 of Intraflagellar transport protein 140 homolog

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 823 of Intraflagellar transport protein 140 homolog

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 Intraflagellar transport protein 140 homolog between cysteines 1198 and 1199. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
8bbg
Structure name
structure of the ift-a complex; anterograde ift-a train model
Structure deposition date
2022-10-12
Thiol separation (Å)
6
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
50
Peptide accession
Q96RY7
Residue number A
1198
Residue number B
1199
Peptide name
Intraflagellar transport protein 140 homolog

Ligandability

Cysteine 1198 of Intraflagellar transport protein 140 homolog

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 1199 of Intraflagellar transport protein 140 homolog

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 Intraflagellar transport protein 140 homolog between cysteines 1159 and 1198. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
8bbg
Structure name
structure of the ift-a complex; anterograde ift-a train model
Structure deposition date
2022-10-12
Thiol separation (Å)
7
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
46
Peptide accession
Q96RY7
Residue number A
1159
Residue number B
1198
Peptide name
Intraflagellar transport protein 140 homolog

Ligandability

Cysteine 1159 of Intraflagellar transport protein 140 homolog

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 1198 of Intraflagellar transport protein 140 homolog

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 Intraflagellar transport protein 140 homolog between cysteines 530 and 577. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
8bbg
Structure name
structure of the ift-a complex; anterograde ift-a train model
Structure deposition date
2022-10-12
Thiol separation (Å)
5
Half-sphere exposure sum ?
92
Minimum pKa ?
14
% buried
100
Peptide accession
Q96RY7
Residue number A
530
Residue number B
577
Peptide name
Intraflagellar transport protein 140 homolog

Ligandability

Cysteine 530 of Intraflagellar transport protein 140 homolog

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 577 of Intraflagellar transport protein 140 homolog

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 Intraflagellar transport protein 140 homolog between cysteines 557 and 559. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
8bbf
Structure name
structure of the ift-a complex; ift-a1 module
Structure deposition date
2022-10-12
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
11
% buried
67
Peptide accession
Q96RY7
Residue number A
557
Residue number B
559
Peptide name
Intraflagellar transport protein 140 homolog

Ligandability

Cysteine 557 of Intraflagellar transport protein 140 homolog

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 559 of Intraflagellar transport protein 140 homolog

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 Intraflagellar transport protein 140 homolog between cysteines 1159 and 1199. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
8bbg
Structure name
structure of the ift-a complex; anterograde ift-a train model
Structure deposition date
2022-10-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
11
% buried
60
Peptide accession
Q96RY7
Residue number A
1159
Residue number B
1199
Peptide name
Intraflagellar transport protein 140 homolog

Ligandability

Cysteine 1159 of Intraflagellar transport protein 140 homolog

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 1199 of Intraflagellar transport protein 140 homolog

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 Intraflagellar transport protein 140 homolog between cysteines 331 and 333. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
8bbg
Structure name
structure of the ift-a complex; anterograde ift-a train model
Structure deposition date
2022-10-12
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
100
Peptide accession
Q96RY7
Residue number A
331
Residue number B
333
Peptide name
Intraflagellar transport protein 140 homolog

Ligandability

Cysteine 331 of Intraflagellar transport protein 140 homolog

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 333 of Intraflagellar transport protein 140 homolog

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 Intraflagellar transport protein 140 homolog between cysteines 68 and 155. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
8bbf
Structure name
structure of the ift-a complex; ift-a1 module
Structure deposition date
2022-10-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
10
% buried
100
Peptide accession
Q96RY7
Residue number A
68
Residue number B
155
Peptide name
Intraflagellar transport protein 140 homolog

Ligandability

Cysteine 68 of Intraflagellar transport protein 140 homolog

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 155 of Intraflagellar transport protein 140 homolog

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 Intraflagellar transport protein 140 homolog between cysteines 329 and 331. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
8bbf
Structure name
structure of the ift-a complex; ift-a1 module
Structure deposition date
2022-10-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
11
% buried
94
Peptide accession
Q96RY7
Residue number A
329
Residue number B
331
Peptide name
Intraflagellar transport protein 140 homolog

Ligandability

Cysteine 329 of Intraflagellar transport protein 140 homolog

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 331 of Intraflagellar transport protein 140 homolog

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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