F-box/LRR-repeat protein 17
Intermolecular
Cysteine 160 of S-phase kinase-associated protein 1 and cysteine 342 L
Intramolecular
Cysteine 396 and cysteine 422
Cysteine 437 and cysteine 463
Cysteine 627 and cysteine 653
Cysteine 602 and cysteine 627
Cysteine 489 and cysteine 515
Cysteine 574 and cysteine 602
Cysteine 463 and cysteine 489
Cysteine 411 and cysteine 437
Cysteine 342 and cysteine 356
More...Cysteine 349 and cysteine 356
Cysteine 574 and cysteine 627
Cysteine 583 and cysteine 602
6w66 A 160 B 342
A redox-regulated disulphide may form between cysteine 160 of S-phase kinase-associated protein 1 and cysteine 342 of F-box/LRR-repeat protein 17.
Details
Redox score ?
79
PDB code
6w66
Structure name
the structure of the f64a, s172a mutant keap1-btb domain in complex with skp1-fbxl17
Structure deposition date
2020-03-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
7
% buried
61
Peptide A name
S-phase kinase-associated protein 1
Peptide B name
F-box/LRR-repeat protein 17
Peptide A accession
P63208
Peptide B accession
Q9UF56
Peptide A residue number
160
Peptide B residue number
342
Ligandability
Cysteine 160 of S-phase kinase-associated protein 1
Cysteine 342 of F-box/LRR-repeat protein 17
6w66 B 396 B 422
A redox-regulated disulphide may form within F-box/LRR-repeat protein 17 between cysteines 396 and 422.
Details
Redox score ?
61
PDB code
6w66
Structure name
the structure of the f64a, s172a mutant keap1-btb domain in complex with skp1-fbxl17
Structure deposition date
2020-03-16
Thiol separation (Å)
5
Half-sphere exposure sum ?
64
Minimum pKa ?
12
% buried
74
Peptide accession
Q9UF56
Residue number A
396
Residue number B
422
Peptide name
F-box/LRR-repeat protein 17
Ligandability
Cysteine 396 of F-box/LRR-repeat protein 17
Cysteine 422 of F-box/LRR-repeat protein 17
6w66 B 437 B 463
A redox-regulated disulphide may form within F-box/LRR-repeat protein 17 between cysteines 437 and 463. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
6w66
Structure name
the structure of the f64a, s172a mutant keap1-btb domain in complex with skp1-fbxl17
Structure deposition date
2020-03-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
78
Peptide accession
Q9UF56
Residue number A
437
Residue number B
463
Peptide name
F-box/LRR-repeat protein 17
Ligandability
Cysteine 437 of F-box/LRR-repeat protein 17
Cysteine 463 of F-box/LRR-repeat protein 17
6w66 B 627 B 653
A redox-regulated disulphide may form within F-box/LRR-repeat protein 17 between cysteines 627 and 653. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
6w66
Structure name
the structure of the f64a, s172a mutant keap1-btb domain in complex with skp1-fbxl17
Structure deposition date
2020-03-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
75
Minimum pKa ?
13
% buried
98
Peptide accession
Q9UF56
Residue number A
627
Residue number B
653
Peptide name
F-box/LRR-repeat protein 17
Ligandability
Cysteine 627 of F-box/LRR-repeat protein 17
Cysteine 653 of F-box/LRR-repeat protein 17
6w66 B 602 B 627
A redox-regulated disulphide may form within F-box/LRR-repeat protein 17 between cysteines 602 and 627. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
6w66
Structure name
the structure of the f64a, s172a mutant keap1-btb domain in complex with skp1-fbxl17
Structure deposition date
2020-03-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
76
Minimum pKa ?
13
% buried
100
Peptide accession
Q9UF56
Residue number A
602
Residue number B
627
Peptide name
F-box/LRR-repeat protein 17
Ligandability
Cysteine 602 of F-box/LRR-repeat protein 17
Cysteine 627 of F-box/LRR-repeat protein 17
6w66 B 489 B 515
A redox-regulated disulphide may form within F-box/LRR-repeat protein 17 between cysteines 489 and 515. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
6w66
Structure name
the structure of the f64a, s172a mutant keap1-btb domain in complex with skp1-fbxl17
Structure deposition date
2020-03-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
70
Peptide accession
Q9UF56
Residue number A
489
Residue number B
515
Peptide name
F-box/LRR-repeat protein 17
Ligandability
Cysteine 489 of F-box/LRR-repeat protein 17
Cysteine 515 of F-box/LRR-repeat protein 17
6w66 B 574 B 602
A redox-regulated disulphide may form within F-box/LRR-repeat protein 17 between cysteines 574 and 602. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
6w66
Structure name
the structure of the f64a, s172a mutant keap1-btb domain in complex with skp1-fbxl17
Structure deposition date
2020-03-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
100
Peptide accession
Q9UF56
Residue number A
574
Residue number B
602
Peptide name
F-box/LRR-repeat protein 17
Ligandability
Cysteine 574 of F-box/LRR-repeat protein 17
Cysteine 602 of F-box/LRR-repeat protein 17
6w66 B 463 B 489
A redox-regulated disulphide may form within F-box/LRR-repeat protein 17 between cysteines 463 and 489. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
6w66
Structure name
the structure of the f64a, s172a mutant keap1-btb domain in complex with skp1-fbxl17
Structure deposition date
2020-03-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
76
Peptide accession
Q9UF56
Residue number A
463
Residue number B
489
Peptide name
F-box/LRR-repeat protein 17
Ligandability
Cysteine 463 of F-box/LRR-repeat protein 17
Cysteine 489 of F-box/LRR-repeat protein 17
6w66 B 411 B 437
A redox-regulated disulphide may form within F-box/LRR-repeat protein 17 between cysteines 411 and 437. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
6w66
Structure name
the structure of the f64a, s172a mutant keap1-btb domain in complex with skp1-fbxl17
Structure deposition date
2020-03-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
70
Peptide accession
Q9UF56
Residue number A
411
Residue number B
437
Peptide name
F-box/LRR-repeat protein 17
Ligandability
Cysteine 411 of F-box/LRR-repeat protein 17
Cysteine 437 of F-box/LRR-repeat protein 17
6w66 B 342 B 356
A redox-regulated disulphide may form within F-box/LRR-repeat protein 17 between cysteines 342 and 356. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
6w66
Structure name
the structure of the f64a, s172a mutant keap1-btb domain in complex with skp1-fbxl17
Structure deposition date
2020-03-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
69
Minimum pKa ?
12
% buried
90
Peptide accession
Q9UF56
Residue number A
342
Residue number B
356
Peptide name
F-box/LRR-repeat protein 17
Ligandability
Cysteine 342 of F-box/LRR-repeat protein 17
Cysteine 356 of F-box/LRR-repeat protein 17
6w66 B 349 B 356
A redox-regulated disulphide may form within F-box/LRR-repeat protein 17 between cysteines 349 and 356. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
6w66
Structure name
the structure of the f64a, s172a mutant keap1-btb domain in complex with skp1-fbxl17
Structure deposition date
2020-03-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
78
Peptide accession
Q9UF56
Residue number A
349
Residue number B
356
Peptide name
F-box/LRR-repeat protein 17
Ligandability
Cysteine 349 of F-box/LRR-repeat protein 17
Cysteine 356 of F-box/LRR-repeat protein 17
6w66 B 574 B 627
A redox-regulated disulphide may form within F-box/LRR-repeat protein 17 between cysteines 574 and 627. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
6w66
Structure name
the structure of the f64a, s172a mutant keap1-btb domain in complex with skp1-fbxl17
Structure deposition date
2020-03-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
100
Peptide accession
Q9UF56
Residue number A
574
Residue number B
627
Peptide name
F-box/LRR-repeat protein 17
Ligandability
Cysteine 574 of F-box/LRR-repeat protein 17
Cysteine 627 of F-box/LRR-repeat protein 17
6w66 B 583 B 602
A redox-regulated disulphide may form within F-box/LRR-repeat protein 17 between cysteines 583 and 602. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
6w66
Structure name
the structure of the f64a, s172a mutant keap1-btb domain in complex with skp1-fbxl17
Structure deposition date
2020-03-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
92
Peptide accession
Q9UF56
Residue number A
583
Residue number B
602
Peptide name
F-box/LRR-repeat protein 17
Ligandability
Cysteine 583 of F-box/LRR-repeat protein 17
Cysteine 602 of F-box/LRR-repeat protein 17
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