S-phase kinase-associated protein 2
Intermolecular
Cysteine 111 and cysteine 120 of S-phase kinase-associated protein 1 L
Cysteine 113 and cysteine 160 of S-phase kinase-associated protein 1 L
Intramolecular
Cysteine 240 and cysteine 266
Cysteine 327 and cysteine 345
Cysteine 111 and cysteine 113
Cysteine 165 and cysteine 414
1fqv A 123 B 120
A redox-regulated disulphide may form between cysteine 111 of S-phase kinase-associated protein 2 and cysteine 120 of S-phase kinase-associated protein 1 (123 and 120 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
1fqv
Structure name
insights into scf ubiquitin ligases from the structure of the skp1-skp2 complex
Structure deposition date
2000-09-06
Thiol separation (Å)
5
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
72
Peptide A name
S-phase kinase-associated protein 2
Peptide B name
S-phase kinase-associated protein 1
Peptide A accession
Q13309
Peptide B accession
P63208
Peptide A residue number
111
Peptide B residue number
120
Ligandability
Cysteine 111 of S-phase kinase-associated protein 2
Cysteine 120 of S-phase kinase-associated protein 1
1fqv M 125 N 160
A redox-regulated disulphide may form between cysteine 113 of S-phase kinase-associated protein 2 and cysteine 160 of S-phase kinase-associated protein 1 (125 and 160 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
1fqv
Structure name
insights into scf ubiquitin ligases from the structure of the skp1-skp2 complex
Structure deposition date
2000-09-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
42
Peptide A name
S-phase kinase-associated protein 2
Peptide B name
S-phase kinase-associated protein 1
Peptide A accession
Q13309
Peptide B accession
P63208
Peptide A residue number
113
Peptide B residue number
160
Ligandability
Cysteine 113 of S-phase kinase-associated protein 2
Cysteine 160 of S-phase kinase-associated protein 1
1fqv G 252 G 278
A redox-regulated disulphide may form within S-phase kinase-associated protein 2 between cysteines 240 and 266 (252 and 278 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
1fqv
Structure name
insights into scf ubiquitin ligases from the structure of the skp1-skp2 complex
Structure deposition date
2000-09-06
Thiol separation (Å)
6
Half-sphere exposure sum ?
70
Minimum pKa ?
12
% buried
100
Peptide accession
Q13309
Residue number A
240
Residue number B
266
Peptide name
S-phase kinase-associated protein 2
Ligandability
Cysteine 240 of S-phase kinase-associated protein 2
Cysteine 266 of S-phase kinase-associated protein 2
1fqv E 339 E 357
A redox-regulated disulphide may form within S-phase kinase-associated protein 2 between cysteines 327 and 345 (339 and 357 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
1fqv
Structure name
insights into scf ubiquitin ligases from the structure of the skp1-skp2 complex
Structure deposition date
2000-09-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
67
Minimum pKa ?
12
% buried
82
Peptide accession
Q13309
Residue number A
327
Residue number B
345
Peptide name
S-phase kinase-associated protein 2
Ligandability
Cysteine 327 of S-phase kinase-associated protein 2
Cysteine 345 of S-phase kinase-associated protein 2
1ldk E 3123 E 3125
A redox-regulated disulphide may form within S-phase kinase-associated protein 2 between cysteines 111 and 113 (3123 and 3125 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
1ldk
Structure name
structure of the cul1-rbx1-skp1-f boxskp2 scf ubiquitin ligase complex
Structure deposition date
2002-04-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
48
Minimum pKa ?
9
% buried
18
Peptide accession
Q13309
Residue number A
111
Residue number B
113
Peptide name
S-phase kinase-associated protein 2
Ligandability
Cysteine 111 of S-phase kinase-associated protein 2
Cysteine 113 of S-phase kinase-associated protein 2
1fqv G 177 G 426
A redox-regulated disulphide may form within S-phase kinase-associated protein 2 between cysteines 165 and 414 (177 and 426 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
29
PDB code
1fqv
Structure name
insights into scf ubiquitin ligases from the structure of the skp1-skp2 complex
Structure deposition date
2000-09-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
89
Peptide accession
Q13309
Residue number A
165
Residue number B
414
Peptide name
S-phase kinase-associated protein 2
Ligandability
Cysteine 165 of S-phase kinase-associated protein 2
Cysteine 414 of S-phase kinase-associated protein 2
If this tool was useful for finding a disulphide, please cite: