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Intraflagellar transport protein 122 homolog

Intramolecular
Cysteine 1060 and cysteine 1077
Cysteine 1057 and cysteine 1060
Cysteine 1207 and cysteine 1229
Cysteine 1074 and cysteine 1077
Cysteine 1057 and cysteine 1074
Cysteine 1060 and cysteine 1074
Cysteine 1057 and cysteine 1077
Cysteine 1229 and cysteine 1232
Cysteine 1207 and cysteine 1232
Cysteine 1210 and cysteine 1229
More...
Cysteine 1210 and cysteine 1232
Cysteine 285 and cysteine 327
Cysteine 111 and cysteine 138
Cysteine 1228 and cysteine 1235
Cysteine 1228 and cysteine 1229
Cysteine 98 and cysteine 138
Cysteine 436 and cysteine 449
Cysteine 569 and cysteine 604
Cysteine 1228 and cysteine 1232
Cysteine 137 and cysteine 138
Cysteine 58 and cysteine 98
Cysteine 58 and cysteine 138
Cysteine 98 and cysteine 137
Cysteine 442 and cysteine 456
Cysteine 1207 and cysteine 1228
Cysteine 784 and cysteine 811
Cysteine 284 and cysteine 285
Cysteine 1207 and cysteine 1210
Cysteine 1232 and cysteine 1235
Cysteine 98 and cysteine 111
Cysteine 284 and cysteine 327
Cysteine 519 and cysteine 538
Cysteine 14 and cysteine 340
Cysteine 564 and cysteine 638
Cysteine 327 and cysteine 340
Cysteine 183 and cysteine 327
Cysteine 111 and cysteine 137
Cysteine 285 and cysteine 340
Cysteine 58 and cysteine 111
A redox-regulated disulphide may form within Intraflagellar transport protein 122 homolog between cysteines 1060 and 1077.

Details

Redox score ?
85
PDB code
8bbf
Structure name
structure of the ift-a complex; ift-a1 module
Structure deposition date
2022-10-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
6
% buried
10
Peptide accession
Q9HBG6
Residue number A
1060
Residue number B
1077
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 1060 of Intraflagellar transport protein 122 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 1077 of Intraflagellar transport protein 122 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 122 homolog between cysteines 1057 and 1060.

Details

Redox score ?
85
PDB code
8bbf
Structure name
structure of the ift-a complex; ift-a1 module
Structure deposition date
2022-10-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
6
% buried
18
Peptide accession
Q9HBG6
Residue number A
1057
Residue number B
1060
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 1057 of Intraflagellar transport protein 122 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 1060 of Intraflagellar transport protein 122 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 122 homolog between cysteines 1207 and 1229.

Details

Redox score ?
81
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)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
7
% buried
nan
Peptide accession
Q9HBG6
Residue number A
1207
Residue number B
1229
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 1207 of Intraflagellar transport protein 122 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 1229 of Intraflagellar transport protein 122 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 122 homolog between cysteines 1074 and 1077.

Details

Redox score ?
80
PDB code
8bbf
Structure name
structure of the ift-a complex; ift-a1 module
Structure deposition date
2022-10-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
16
Peptide accession
Q9HBG6
Residue number A
1074
Residue number B
1077
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 1074 of Intraflagellar transport protein 122 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 1077 of Intraflagellar transport protein 122 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 122 homolog between cysteines 1057 and 1074.

Details

Redox score ?
78
PDB code
8bbf
Structure name
structure of the ift-a complex; ift-a1 module
Structure deposition date
2022-10-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
24
Peptide accession
Q9HBG6
Residue number A
1057
Residue number B
1074
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 1057 of Intraflagellar transport protein 122 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 1074 of Intraflagellar transport protein 122 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 122 homolog between cysteines 1060 and 1074.

Details

Redox score ?
77
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)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
9
% buried
34
Peptide accession
Q9HBG6
Residue number A
1060
Residue number B
1074
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 1060 of Intraflagellar transport protein 122 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 1074 of Intraflagellar transport protein 122 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 122 homolog between cysteines 1057 and 1077.

Details

Redox score ?
77
PDB code
8bbf
Structure name
structure of the ift-a complex; ift-a1 module
Structure deposition date
2022-10-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
10
% buried
26
Peptide accession
Q9HBG6
Residue number A
1057
Residue number B
1077
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 1057 of Intraflagellar transport protein 122 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 1077 of Intraflagellar transport protein 122 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 122 homolog between cysteines 1229 and 1232.

Details

Redox score ?
77
PDB code
8bbf
Structure name
structure of the ift-a complex; ift-a1 module
Structure deposition date
2022-10-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
8
% buried
71
Peptide accession
Q9HBG6
Residue number A
1229
Residue number B
1232
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 1229 of Intraflagellar transport protein 122 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 1232 of Intraflagellar transport protein 122 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 122 homolog between cysteines 1207 and 1232.

Details

Redox score ?
76
PDB code
8bbf
Structure name
structure of the ift-a complex; ift-a1 module
Structure deposition date
2022-10-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
8
% buried
nan
Peptide accession
Q9HBG6
Residue number A
1207
Residue number B
1232
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 1207 of Intraflagellar transport protein 122 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 1232 of Intraflagellar transport protein 122 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 122 homolog between cysteines 1210 and 1229.

Details

Redox score ?
75
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)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
7
% buried
88
Peptide accession
Q9HBG6
Residue number A
1210
Residue number B
1229
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 1210 of Intraflagellar transport protein 122 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 1229 of Intraflagellar transport protein 122 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 122 homolog between cysteines 1210 and 1232.

Details

Redox score ?
72
PDB code
8bbf
Structure name
structure of the ift-a complex; ift-a1 module
Structure deposition date
2022-10-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
8
% buried
80
Peptide accession
Q9HBG6
Residue number A
1210
Residue number B
1232
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 1210 of Intraflagellar transport protein 122 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 1232 of Intraflagellar transport protein 122 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 122 homolog between cysteines 285 and 327.

Details

Redox score ?
69
PDB code
8bbe
Structure name
structure of the ift-a complex; ift-a2 module
Structure deposition date
2022-10-12
Thiol separation (Å)
3
Half-sphere exposure sum ?
87
Minimum pKa ?
9
% buried
100
Peptide accession
Q9HBG6
Residue number A
285
Residue number B
327
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 285 of Intraflagellar transport protein 122 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 327 of Intraflagellar transport protein 122 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 122 homolog between cysteines 111 and 138.

Details

Redox score ?
67
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)
4
Half-sphere exposure sum ?
92
Minimum pKa ?
8
% buried
100
Peptide accession
Q9HBG6
Residue number A
111
Residue number B
138
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 111 of Intraflagellar transport protein 122 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 138 of Intraflagellar transport protein 122 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 122 homolog between cysteines 1228 and 1235.

Details

Redox score ?
65
PDB code
8bbf
Structure name
structure of the ift-a complex; ift-a1 module
Structure deposition date
2022-10-12
Thiol separation (Å)
6
Half-sphere exposure sum ?
46
Minimum pKa ?
10
% buried
12
Peptide accession
Q9HBG6
Residue number A
1228
Residue number B
1235
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 1228 of Intraflagellar transport protein 122 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 1235 of Intraflagellar transport protein 122 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 122 homolog between cysteines 1228 and 1229. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
60
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 ?
55
Minimum pKa ?
7
% buried
52
Peptide accession
Q9HBG6
Residue number A
1228
Residue number B
1229
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 1228 of Intraflagellar transport protein 122 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 1229 of Intraflagellar transport protein 122 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 122 homolog between cysteines 98 and 138. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
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 ?
88
Minimum pKa ?
8
% buried
100
Peptide accession
Q9HBG6
Residue number A
98
Residue number B
138
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 98 of Intraflagellar transport protein 122 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 138 of Intraflagellar transport protein 122 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 122 homolog between cysteines 436 and 449. 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 ?
58
Minimum pKa ?
11
% buried
60
Peptide accession
Q9HBG6
Residue number A
436
Residue number B
449
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 436 of Intraflagellar transport protein 122 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 449 of Intraflagellar transport protein 122 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 122 homolog between cysteines 569 and 604. 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)
6
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
90
Peptide accession
Q9HBG6
Residue number A
569
Residue number B
604
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 569 of Intraflagellar transport protein 122 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 604 of Intraflagellar transport protein 122 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 122 homolog between cysteines 1228 and 1232. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
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 ?
57
Minimum pKa ?
9
% buried
50
Peptide accession
Q9HBG6
Residue number A
1228
Residue number B
1232
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 1228 of Intraflagellar transport protein 122 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 1232 of Intraflagellar transport protein 122 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 122 homolog between cysteines 137 and 138. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
8bbe
Structure name
structure of the ift-a complex; ift-a2 module
Structure deposition date
2022-10-12
Thiol separation (Å)
7
Half-sphere exposure sum ?
91
Minimum pKa ?
8
% buried
100
Peptide accession
Q9HBG6
Residue number A
137
Residue number B
138
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 137 of Intraflagellar transport protein 122 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 138 of Intraflagellar transport protein 122 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 122 homolog between cysteines 58 and 98. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
8bbe
Structure name
structure of the ift-a complex; ift-a2 module
Structure deposition date
2022-10-12
Thiol separation (Å)
5
Half-sphere exposure sum ?
92
Minimum pKa ?
11
% buried
100
Peptide accession
Q9HBG6
Residue number A
58
Residue number B
98
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 58 of Intraflagellar transport protein 122 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 98 of Intraflagellar transport protein 122 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 122 homolog between cysteines 58 and 138. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
8bbe
Structure name
structure of the ift-a complex; ift-a2 module
Structure deposition date
2022-10-12
Thiol separation (Å)
7
Half-sphere exposure sum ?
90
Minimum pKa ?
8
% buried
100
Peptide accession
Q9HBG6
Residue number A
58
Residue number B
138
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 58 of Intraflagellar transport protein 122 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 138 of Intraflagellar transport protein 122 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 122 homolog between cysteines 98 and 137. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
8bbe
Structure name
structure of the ift-a complex; ift-a2 module
Structure deposition date
2022-10-12
Thiol separation (Å)
6
Half-sphere exposure sum ?
93
Minimum pKa ?
11
% buried
100
Peptide accession
Q9HBG6
Residue number A
98
Residue number B
137
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 98 of Intraflagellar transport protein 122 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 137 of Intraflagellar transport protein 122 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 122 homolog between cysteines 442 and 456. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
8bbe
Structure name
structure of the ift-a complex; ift-a2 module
Structure deposition date
2022-10-12
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
82
Peptide accession
Q9HBG6
Residue number A
442
Residue number B
456
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 442 of Intraflagellar transport protein 122 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 456 of Intraflagellar transport protein 122 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 122 homolog between cysteines 1207 and 1228. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
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 ?
55
Minimum pKa ?
9
% buried
nan
Peptide accession
Q9HBG6
Residue number A
1207
Residue number B
1228
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 1207 of Intraflagellar transport protein 122 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 1228 of Intraflagellar transport protein 122 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 122 homolog between cysteines 784 and 811. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
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 ?
81
Minimum pKa ?
11
% buried
61
Peptide accession
Q9HBG6
Residue number A
784
Residue number B
811
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 784 of Intraflagellar transport protein 122 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 811 of Intraflagellar transport protein 122 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 122 homolog between cysteines 284 and 285. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
8bbe
Structure name
structure of the ift-a complex; ift-a2 module
Structure deposition date
2022-10-12
Thiol separation (Å)
6
Half-sphere exposure sum ?
90
Minimum pKa ?
14
% buried
100
Peptide accession
Q9HBG6
Residue number A
284
Residue number B
285
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 284 of Intraflagellar transport protein 122 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 285 of Intraflagellar transport protein 122 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 122 homolog between cysteines 1207 and 1210. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
8bbf
Structure name
structure of the ift-a complex; ift-a1 module
Structure deposition date
2022-10-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
26
% buried
nan
Peptide accession
Q9HBG6
Residue number A
1207
Residue number B
1210
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 1207 of Intraflagellar transport protein 122 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 1210 of Intraflagellar transport protein 122 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 122 homolog between cysteines 1232 and 1235. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
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 ?
57
Minimum pKa ?
10
% buried
36
Peptide accession
Q9HBG6
Residue number A
1232
Residue number B
1235
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 1232 of Intraflagellar transport protein 122 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 1235 of Intraflagellar transport protein 122 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 122 homolog between cysteines 98 and 111. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
8bbe
Structure name
structure of the ift-a complex; ift-a2 module
Structure deposition date
2022-10-12
Thiol separation (Å)
7
Half-sphere exposure sum ?
94
Minimum pKa ?
11
% buried
100
Peptide accession
Q9HBG6
Residue number A
98
Residue number B
111
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 98 of Intraflagellar transport protein 122 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 111 of Intraflagellar transport protein 122 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 122 homolog between cysteines 284 and 327. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
8bbe
Structure name
structure of the ift-a complex; ift-a2 module
Structure deposition date
2022-10-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
90
Minimum pKa ?
9
% buried
100
Peptide accession
Q9HBG6
Residue number A
284
Residue number B
327
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 284 of Intraflagellar transport protein 122 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 327 of Intraflagellar transport protein 122 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 122 homolog between cysteines 519 and 538. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
8bbe
Structure name
structure of the ift-a complex; ift-a2 module
Structure deposition date
2022-10-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
10
% buried
96
Peptide accession
Q9HBG6
Residue number A
519
Residue number B
538
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 519 of Intraflagellar transport protein 122 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 538 of Intraflagellar transport protein 122 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 122 homolog between cysteines 14 and 340. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
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)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
82
Peptide accession
Q9HBG6
Residue number A
14
Residue number B
340
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 14 of Intraflagellar transport protein 122 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 340 of Intraflagellar transport protein 122 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 122 homolog between cysteines 564 and 638. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
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 ?
70
Minimum pKa ?
10
% buried
86
Peptide accession
Q9HBG6
Residue number A
564
Residue number B
638
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 564 of Intraflagellar transport protein 122 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 638 of Intraflagellar transport protein 122 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 122 homolog between cysteines 327 and 340. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
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 ?
88
Minimum pKa ?
9
% buried
88
Peptide accession
Q9HBG6
Residue number A
327
Residue number B
340
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 327 of Intraflagellar transport protein 122 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 340 of Intraflagellar transport protein 122 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 122 homolog between cysteines 183 and 327. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
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 ?
86
Minimum pKa ?
9
% buried
100
Peptide accession
Q9HBG6
Residue number A
183
Residue number B
327
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 183 of Intraflagellar transport protein 122 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 327 of Intraflagellar transport protein 122 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 122 homolog between cysteines 111 and 137. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
8bbe
Structure name
structure of the ift-a complex; ift-a2 module
Structure deposition date
2022-10-12
Thiol separation (Å)
8
Half-sphere exposure sum ?
97
Minimum pKa ?
13
% buried
100
Peptide accession
Q9HBG6
Residue number A
111
Residue number B
137
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 111 of Intraflagellar transport protein 122 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 137 of Intraflagellar transport protein 122 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 122 homolog between cysteines 285 and 340. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
8bbe
Structure name
structure of the ift-a complex; ift-a2 module
Structure deposition date
2022-10-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
88
Peptide accession
Q9HBG6
Residue number A
285
Residue number B
340
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 285 of Intraflagellar transport protein 122 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 340 of Intraflagellar transport protein 122 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 122 homolog between cysteines 58 and 111. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
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 ?
96
Minimum pKa ?
14
% buried
100
Peptide accession
Q9HBG6
Residue number A
58
Residue number B
111
Peptide name
Intraflagellar transport protein 122 homolog

Ligandability

Cysteine 58 of Intraflagellar transport protein 122 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 111 of Intraflagellar transport protein 122 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.

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

Coleman, P. et al. (2026). ReDisulphID: A discovery platform for thiol redox sensors identifies a druggable site regulating p53 activation. Redox Biology.