E3 SUMO-protein ligase PIAS2
Intramolecular
Cysteine 362 and cysteine 385 L
Cysteine 362 and cysteine 388 L
Cysteine 385 and cysteine 388 L
Cysteine 357 and cysteine 367
Cysteine 357 and cysteine 362
Cysteine 362 and cysteine 367
Cysteine 357 and cysteine 385 L
Cysteine 367 and cysteine 385 L
Cysteine 346 and cysteine 357
Cysteine 214 and cysteine 220
Cysteine 346 and cysteine 367
4fo9 A 362 A 385
A redox-regulated disulphide may form within E3 SUMO-protein ligase PIAS2 between cysteines 362 and 385.
Details
Redox score ?
77
PDB code
4fo9
Structure name
crystal structure of the e3 sumo ligase pias2
Structure deposition date
2012-06-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75928
Residue number A
362
Residue number B
385
Peptide name
E3 SUMO-protein ligase PIAS2
Ligandability
Cysteine 362 of E3 SUMO-protein ligase PIAS2
Cysteine 385 of E3 SUMO-protein ligase PIAS2
4fo9 A 362 A 388
A redox-regulated disulphide may form within E3 SUMO-protein ligase PIAS2 between cysteines 362 and 388.
Details
Redox score ?
76
PDB code
4fo9
Structure name
crystal structure of the e3 sumo ligase pias2
Structure deposition date
2012-06-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75928
Residue number A
362
Residue number B
388
Peptide name
E3 SUMO-protein ligase PIAS2
Ligandability
Cysteine 362 of E3 SUMO-protein ligase PIAS2
Cysteine 388 of E3 SUMO-protein ligase PIAS2
4fo9 A 385 A 388
A redox-regulated disulphide may form within E3 SUMO-protein ligase PIAS2 between cysteines 385 and 388.
Details
Redox score ?
74
PDB code
4fo9
Structure name
crystal structure of the e3 sumo ligase pias2
Structure deposition date
2012-06-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75928
Residue number A
385
Residue number B
388
Peptide name
E3 SUMO-protein ligase PIAS2
Ligandability
Cysteine 385 of E3 SUMO-protein ligase PIAS2
Cysteine 388 of E3 SUMO-protein ligase PIAS2
4fo9 A 357 A 367
A redox-regulated disulphide may form within E3 SUMO-protein ligase PIAS2 between cysteines 357 and 367. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
4fo9
Structure name
crystal structure of the e3 sumo ligase pias2
Structure deposition date
2012-06-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75928
Residue number A
357
Residue number B
367
Peptide name
E3 SUMO-protein ligase PIAS2
Ligandability
Cysteine 357 of E3 SUMO-protein ligase PIAS2
Cysteine 367 of E3 SUMO-protein ligase PIAS2
4fo9 A 357 A 362
A redox-regulated disulphide may form within E3 SUMO-protein ligase PIAS2 between cysteines 357 and 362. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
4fo9
Structure name
crystal structure of the e3 sumo ligase pias2
Structure deposition date
2012-06-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75928
Residue number A
357
Residue number B
362
Peptide name
E3 SUMO-protein ligase PIAS2
Ligandability
Cysteine 357 of E3 SUMO-protein ligase PIAS2
Cysteine 362 of E3 SUMO-protein ligase PIAS2
4fo9 A 362 A 367
A redox-regulated disulphide may form within E3 SUMO-protein ligase PIAS2 between cysteines 362 and 367. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
4fo9
Structure name
crystal structure of the e3 sumo ligase pias2
Structure deposition date
2012-06-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75928
Residue number A
362
Residue number B
367
Peptide name
E3 SUMO-protein ligase PIAS2
Ligandability
Cysteine 362 of E3 SUMO-protein ligase PIAS2
Cysteine 367 of E3 SUMO-protein ligase PIAS2
4fo9 A 357 A 385
A redox-regulated disulphide may form within E3 SUMO-protein ligase PIAS2 between cysteines 357 and 385. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
4fo9
Structure name
crystal structure of the e3 sumo ligase pias2
Structure deposition date
2012-06-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75928
Residue number A
357
Residue number B
385
Peptide name
E3 SUMO-protein ligase PIAS2
Ligandability
Cysteine 357 of E3 SUMO-protein ligase PIAS2
Cysteine 385 of E3 SUMO-protein ligase PIAS2
4fo9 A 367 A 385
A redox-regulated disulphide may form within E3 SUMO-protein ligase PIAS2 between cysteines 367 and 385. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
4fo9
Structure name
crystal structure of the e3 sumo ligase pias2
Structure deposition date
2012-06-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75928
Residue number A
367
Residue number B
385
Peptide name
E3 SUMO-protein ligase PIAS2
Ligandability
Cysteine 367 of E3 SUMO-protein ligase PIAS2
Cysteine 385 of E3 SUMO-protein ligase PIAS2
4fo9 A 346 A 357
A redox-regulated disulphide may form within E3 SUMO-protein ligase PIAS2 between cysteines 346 and 357. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
4fo9
Structure name
crystal structure of the e3 sumo ligase pias2
Structure deposition date
2012-06-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75928
Residue number A
346
Residue number B
357
Peptide name
E3 SUMO-protein ligase PIAS2
Ligandability
Cysteine 346 of E3 SUMO-protein ligase PIAS2
Cysteine 357 of E3 SUMO-protein ligase PIAS2
4fo9 A 214 A 220
A redox-regulated disulphide may form within E3 SUMO-protein ligase PIAS2 between cysteines 214 and 220. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
4fo9
Structure name
crystal structure of the e3 sumo ligase pias2
Structure deposition date
2012-06-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75928
Residue number A
214
Residue number B
220
Peptide name
E3 SUMO-protein ligase PIAS2
Ligandability
Cysteine 214 of E3 SUMO-protein ligase PIAS2
Cysteine 220 of E3 SUMO-protein ligase PIAS2
4fo9 A 346 A 367
A redox-regulated disulphide may form within E3 SUMO-protein ligase PIAS2 between cysteines 346 and 367. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
4fo9
Structure name
crystal structure of the e3 sumo ligase pias2
Structure deposition date
2012-06-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75928
Residue number A
346
Residue number B
367
Peptide name
E3 SUMO-protein ligase PIAS2
Ligandability
Cysteine 346 of E3 SUMO-protein ligase PIAS2
Cysteine 367 of E3 SUMO-protein ligase PIAS2
If this tool was useful for finding a disulphide, please cite: