Intraflagellar transport protein 122 homolog
A redox-regulated disulphide may form within Intraflagellar transport protein 122 homolog between cysteines 1060 and 1077.
Details
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
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
Cysteine 1077 of Intraflagellar transport protein 122 homolog
A redox-regulated disulphide may form within Intraflagellar transport protein 122 homolog between cysteines 1057 and 1060.
Details
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
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
Cysteine 1060 of Intraflagellar transport protein 122 homolog
A redox-regulated disulphide may form within Intraflagellar transport protein 122 homolog between cysteines 1207 and 1229.
Details
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
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
Cysteine 1229 of Intraflagellar transport protein 122 homolog
A redox-regulated disulphide may form within Intraflagellar transport protein 122 homolog between cysteines 1074 and 1077.
Details
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
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
Cysteine 1077 of Intraflagellar transport protein 122 homolog
A redox-regulated disulphide may form within Intraflagellar transport protein 122 homolog between cysteines 1057 and 1074.
Details
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
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
Cysteine 1074 of Intraflagellar transport protein 122 homolog
A redox-regulated disulphide may form within Intraflagellar transport protein 122 homolog between cysteines 1060 and 1074.
Details
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
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
Cysteine 1074 of Intraflagellar transport protein 122 homolog
A redox-regulated disulphide may form within Intraflagellar transport protein 122 homolog between cysteines 1057 and 1077.
Details
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
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
Cysteine 1077 of Intraflagellar transport protein 122 homolog
A redox-regulated disulphide may form within Intraflagellar transport protein 122 homolog between cysteines 1229 and 1232.
Details
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
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
Cysteine 1232 of Intraflagellar transport protein 122 homolog
A redox-regulated disulphide may form within Intraflagellar transport protein 122 homolog between cysteines 1207 and 1232.
Details
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
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
Cysteine 1232 of Intraflagellar transport protein 122 homolog
A redox-regulated disulphide may form within Intraflagellar transport protein 122 homolog between cysteines 1210 and 1229.
Details
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
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
Cysteine 1229 of Intraflagellar transport protein 122 homolog
A redox-regulated disulphide may form within Intraflagellar transport protein 122 homolog between cysteines 1210 and 1232.
Details
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
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
Cysteine 1232 of Intraflagellar transport protein 122 homolog
A redox-regulated disulphide may form within Intraflagellar transport protein 122 homolog between cysteines 285 and 327.
Details
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
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
Cysteine 327 of Intraflagellar transport protein 122 homolog
A redox-regulated disulphide may form within Intraflagellar transport protein 122 homolog between cysteines 111 and 138.
Details
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
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
Cysteine 138 of Intraflagellar transport protein 122 homolog
A redox-regulated disulphide may form within Intraflagellar transport protein 122 homolog between cysteines 1228 and 1235.
Details
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
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
Cysteine 1235 of Intraflagellar transport protein 122 homolog
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
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
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
Cysteine 1229 of Intraflagellar transport protein 122 homolog
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
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
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
Cysteine 138 of Intraflagellar transport protein 122 homolog
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
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
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
Cysteine 449 of Intraflagellar transport protein 122 homolog
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
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
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
Cysteine 604 of Intraflagellar transport protein 122 homolog
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
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
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
Cysteine 1232 of Intraflagellar transport protein 122 homolog
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
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
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
Cysteine 138 of Intraflagellar transport protein 122 homolog
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
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
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
Cysteine 98 of Intraflagellar transport protein 122 homolog
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
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
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
Cysteine 138 of Intraflagellar transport protein 122 homolog
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
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
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
Cysteine 137 of Intraflagellar transport protein 122 homolog
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
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
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
Cysteine 456 of Intraflagellar transport protein 122 homolog
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
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
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
Cysteine 1228 of Intraflagellar transport protein 122 homolog
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
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
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
Cysteine 811 of Intraflagellar transport protein 122 homolog
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
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
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
Cysteine 285 of Intraflagellar transport protein 122 homolog
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
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
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
Cysteine 1210 of Intraflagellar transport protein 122 homolog
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
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
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
Cysteine 1235 of Intraflagellar transport protein 122 homolog
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
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
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
Cysteine 111 of Intraflagellar transport protein 122 homolog
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
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
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
Cysteine 327 of Intraflagellar transport protein 122 homolog
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
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
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
Cysteine 538 of Intraflagellar transport protein 122 homolog
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
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
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
Cysteine 340 of Intraflagellar transport protein 122 homolog
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
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
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
Cysteine 638 of Intraflagellar transport protein 122 homolog
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
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
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
Cysteine 340 of Intraflagellar transport protein 122 homolog
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
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
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
Cysteine 327 of Intraflagellar transport protein 122 homolog
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
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
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
Cysteine 137 of Intraflagellar transport protein 122 homolog
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
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
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
Cysteine 340 of Intraflagellar transport protein 122 homolog
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
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
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
Cysteine 111 of Intraflagellar transport protein 122 homolog
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