ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

F-box/LRR-repeat protein 2

Intermolecular
Cysteine 33 and cysteine 160 of S-phase kinase-associated protein 1 L
Intramolecular
Cysteine 230 and cysteine 259
Cysteine 259 and cysteine 285
Cysteine 88 and cysteine 114
Cysteine 192 and cysteine 218
Cysteine 296 and cysteine 322
Cysteine 322 and cysteine 351
Cysteine 270 and cysteine 296
Cysteine 244 and cysteine 270
Cysteine 218 and cysteine 244
More...
Cysteine 351 and cysteine 376
Cysteine 233 and cysteine 259
Cysteine 76 and cysteine 103
Cysteine 140 and cysteine 166
Cysteine 114 and cysteine 140
Cysteine 166 and cysteine 192
Cysteine 207 and cysteine 233
Cysteine 129 and cysteine 155
Cysteine 155 and cysteine 181
Cysteine 338 and cysteine 365
Cysteine 285 and cysteine 311
Cysteine 311 and cysteine 338
Cysteine 240 and cysteine 244
Cysteine 103 and cysteine 129
Cysteine 181 and cysteine 207
Cysteine 122 and cysteine 155
Cysteine 230 and cysteine 233
Cysteine 122 and cysteine 140
Cysteine 240 and cysteine 270
Cysteine 230 and cysteine 285
Cysteine 33 and cysteine 76
Cysteine 122 and cysteine 166
Cysteine 218 and cysteine 240
Cysteine 33 and cysteine 35
A redox-regulated disulphide may form between cysteine 33 of F-box/LRR-repeat protein 2 and cysteine 160 of S-phase kinase-associated protein 1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
56
Peptide A name
F-box/LRR-repeat protein 2
Peptide B name
S-phase kinase-associated protein 1
Peptide A accession
Q9UKC9
Peptide B accession
P63208
Peptide A residue number
33
Peptide B residue number
160

Ligandability

Cysteine 33 of F-box/LRR-repeat protein 2

Cysteine 160 of S-phase kinase-associated protein 1

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 230 and 259.

Details

Redox score ?
70
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
83
Minimum pKa ?
8
% buried
85
Peptide accession
Q9UKC9
Residue number A
230
Residue number B
259
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 230 of F-box/LRR-repeat protein 2

Cysteine 259 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 259 and 285. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
8
% buried
78
Peptide accession
Q9UKC9
Residue number A
259
Residue number B
285
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 259 of F-box/LRR-repeat protein 2

Cysteine 285 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 88 and 114. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
92
Peptide accession
Q9UKC9
Residue number A
88
Residue number B
114
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 88 of F-box/LRR-repeat protein 2

Cysteine 114 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 192 and 218. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
5
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
94
Peptide accession
Q9UKC9
Residue number A
192
Residue number B
218
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 192 of F-box/LRR-repeat protein 2

Cysteine 218 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 296 and 322. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
92
Peptide accession
Q9UKC9
Residue number A
296
Residue number B
322
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 296 of F-box/LRR-repeat protein 2

Cysteine 322 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 322 and 351. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
96
Peptide accession
Q9UKC9
Residue number A
322
Residue number B
351
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 322 of F-box/LRR-repeat protein 2

Cysteine 351 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 270 and 296. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
88
Peptide accession
Q9UKC9
Residue number A
270
Residue number B
296
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 270 of F-box/LRR-repeat protein 2

Cysteine 296 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 244 and 270. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
86
Peptide accession
Q9UKC9
Residue number A
244
Residue number B
270
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 244 of F-box/LRR-repeat protein 2

Cysteine 270 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 218 and 244. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
88
Peptide accession
Q9UKC9
Residue number A
218
Residue number B
244
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 218 of F-box/LRR-repeat protein 2

Cysteine 244 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 351 and 376. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
79
Minimum pKa ?
13
% buried
98
Peptide accession
Q9UKC9
Residue number A
351
Residue number B
376
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 351 of F-box/LRR-repeat protein 2

Cysteine 376 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 233 and 259. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
82
Minimum pKa ?
8
% buried
80
Peptide accession
Q9UKC9
Residue number A
233
Residue number B
259
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 233 of F-box/LRR-repeat protein 2

Cysteine 259 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 76 and 103. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
7
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
73
Peptide accession
Q9UKC9
Residue number A
76
Residue number B
103
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 76 of F-box/LRR-repeat protein 2

Cysteine 103 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 140 and 166. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
100
Peptide accession
Q9UKC9
Residue number A
140
Residue number B
166
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 140 of F-box/LRR-repeat protein 2

Cysteine 166 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 114 and 140. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
77
Minimum pKa ?
13
% buried
100
Peptide accession
Q9UKC9
Residue number A
114
Residue number B
140
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 114 of F-box/LRR-repeat protein 2

Cysteine 140 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 166 and 192. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
100
Peptide accession
Q9UKC9
Residue number A
166
Residue number B
192
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 166 of F-box/LRR-repeat protein 2

Cysteine 192 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 207 and 233. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
84
Peptide accession
Q9UKC9
Residue number A
207
Residue number B
233
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 207 of F-box/LRR-repeat protein 2

Cysteine 233 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 129 and 155. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
7
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
87
Peptide accession
Q9UKC9
Residue number A
129
Residue number B
155
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 129 of F-box/LRR-repeat protein 2

Cysteine 155 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 155 and 181. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
7
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
86
Peptide accession
Q9UKC9
Residue number A
155
Residue number B
181
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 155 of F-box/LRR-repeat protein 2

Cysteine 181 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 338 and 365. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
79
Peptide accession
Q9UKC9
Residue number A
338
Residue number B
365
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 338 of F-box/LRR-repeat protein 2

Cysteine 365 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 285 and 311. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
7
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
82
Peptide accession
Q9UKC9
Residue number A
285
Residue number B
311
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 285 of F-box/LRR-repeat protein 2

Cysteine 311 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 311 and 338. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
82
Peptide accession
Q9UKC9
Residue number A
311
Residue number B
338
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 311 of F-box/LRR-repeat protein 2

Cysteine 338 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 240 and 244. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
7
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
86
Peptide accession
Q9UKC9
Residue number A
240
Residue number B
244
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 240 of F-box/LRR-repeat protein 2

Cysteine 244 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 103 and 129. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
78
Peptide accession
Q9UKC9
Residue number A
103
Residue number B
129
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 103 of F-box/LRR-repeat protein 2

Cysteine 129 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 181 and 207. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
86
Peptide accession
Q9UKC9
Residue number A
181
Residue number B
207
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 181 of F-box/LRR-repeat protein 2

Cysteine 207 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 122 and 155. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
94
Peptide accession
Q9UKC9
Residue number A
122
Residue number B
155
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 122 of F-box/LRR-repeat protein 2

Cysteine 155 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 230 and 233. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
86
Peptide accession
Q9UKC9
Residue number A
230
Residue number B
233
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 230 of F-box/LRR-repeat protein 2

Cysteine 233 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 122 and 140. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
100
Peptide accession
Q9UKC9
Residue number A
122
Residue number B
140
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 122 of F-box/LRR-repeat protein 2

Cysteine 140 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 240 and 270. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
85
Peptide accession
Q9UKC9
Residue number A
240
Residue number B
270
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 240 of F-box/LRR-repeat protein 2

Cysteine 270 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 230 and 285. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
84
Peptide accession
Q9UKC9
Residue number A
230
Residue number B
285
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 230 of F-box/LRR-repeat protein 2

Cysteine 285 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 33 and 76. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
76
Peptide accession
Q9UKC9
Residue number A
33
Residue number B
76
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 33 of F-box/LRR-repeat protein 2

Cysteine 76 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 122 and 166. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
100
Peptide accession
Q9UKC9
Residue number A
122
Residue number B
166
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 122 of F-box/LRR-repeat protein 2

Cysteine 166 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 218 and 240. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
88
Peptide accession
Q9UKC9
Residue number A
218
Residue number B
240
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 218 of F-box/LRR-repeat protein 2

Cysteine 240 of F-box/LRR-repeat protein 2

A redox-regulated disulphide may form within F-box/LRR-repeat protein 2 between cysteines 33 and 35. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
6o60
Structure name
crystal structure of ggtase3-fbxl2-skp1 complex
Structure deposition date
2019-03-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
88
Peptide accession
Q9UKC9
Residue number A
33
Residue number B
35
Peptide name
F-box/LRR-repeat protein 2

Ligandability

Cysteine 33 of F-box/LRR-repeat protein 2

Cysteine 35 of F-box/LRR-repeat protein 2

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