SUMO-specific isopeptidase USPL1
Intramolecular
Cysteine 364 and cysteine 397
Cysteine 361 and cysteine 364
Cysteine 361 and cysteine 397
Cysteine 364 and cysteine 400
Cysteine 361 and cysteine 400
Cysteine 397 and cysteine 400
Cysteine 226 and cysteine 471
Cysteine 226 and cysteine 478
Cysteine 236 and cysteine 240
7p99 A 364 A 397
A redox-regulated disulphide may form within SUMO-specific isopeptidase USPL1 between cysteines 364 and 397.
Details
Redox score ?
87
PDB code
7p99
Structure name
structure of human uspl1 in complex with sumo2
Structure deposition date
2021-07-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
6
% buried
0
Peptide accession
Q5W0Q7
Residue number A
364
Residue number B
397
Peptide name
SUMO-specific isopeptidase USPL1
Ligandability
Cysteine 364 of SUMO-specific isopeptidase USPL1
Cysteine 397 of SUMO-specific isopeptidase USPL1
7p99 A 361 A 364
A redox-regulated disulphide may form within SUMO-specific isopeptidase USPL1 between cysteines 361 and 364.
Details
Redox score ?
87
PDB code
7p99
Structure name
structure of human uspl1 in complex with sumo2
Structure deposition date
2021-07-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
6
% buried
0
Peptide accession
Q5W0Q7
Residue number A
361
Residue number B
364
Peptide name
SUMO-specific isopeptidase USPL1
Ligandability
Cysteine 361 of SUMO-specific isopeptidase USPL1
Cysteine 364 of SUMO-specific isopeptidase USPL1
7p99 A 361 A 397
A redox-regulated disulphide may form within SUMO-specific isopeptidase USPL1 between cysteines 361 and 397.
Details
Redox score ?
86
PDB code
7p99
Structure name
structure of human uspl1 in complex with sumo2
Structure deposition date
2021-07-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
7
% buried
0
Peptide accession
Q5W0Q7
Residue number A
361
Residue number B
397
Peptide name
SUMO-specific isopeptidase USPL1
Ligandability
Cysteine 361 of SUMO-specific isopeptidase USPL1
Cysteine 397 of SUMO-specific isopeptidase USPL1
7p99 A 364 A 400
A redox-regulated disulphide may form within SUMO-specific isopeptidase USPL1 between cysteines 364 and 400.
Details
Redox score ?
86
PDB code
7p99
Structure name
structure of human uspl1 in complex with sumo2
Structure deposition date
2021-07-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
6
% buried
0
Peptide accession
Q5W0Q7
Residue number A
364
Residue number B
400
Peptide name
SUMO-specific isopeptidase USPL1
Ligandability
Cysteine 364 of SUMO-specific isopeptidase USPL1
Cysteine 400 of SUMO-specific isopeptidase USPL1
7p99 A 361 A 400
A redox-regulated disulphide may form within SUMO-specific isopeptidase USPL1 between cysteines 361 and 400.
Details
Redox score ?
85
PDB code
7p99
Structure name
structure of human uspl1 in complex with sumo2
Structure deposition date
2021-07-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
7
% buried
0
Peptide accession
Q5W0Q7
Residue number A
361
Residue number B
400
Peptide name
SUMO-specific isopeptidase USPL1
Ligandability
Cysteine 361 of SUMO-specific isopeptidase USPL1
Cysteine 400 of SUMO-specific isopeptidase USPL1
7p99 A 397 A 400
A redox-regulated disulphide may form within SUMO-specific isopeptidase USPL1 between cysteines 397 and 400.
Details
Redox score ?
80
PDB code
7p99
Structure name
structure of human uspl1 in complex with sumo2
Structure deposition date
2021-07-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
9
% buried
0
Peptide accession
Q5W0Q7
Residue number A
397
Residue number B
400
Peptide name
SUMO-specific isopeptidase USPL1
Ligandability
Cysteine 397 of SUMO-specific isopeptidase USPL1
Cysteine 400 of SUMO-specific isopeptidase USPL1
7p99 A 226 A 471
A redox-regulated disulphide may form within SUMO-specific isopeptidase USPL1 between cysteines 226 and 471.
Details
Redox score ?
78
PDB code
7p99
Structure name
structure of human uspl1 in complex with sumo2
Structure deposition date
2021-07-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
3
% buried
92
Peptide accession
Q5W0Q7
Residue number A
226
Residue number B
471
Peptide name
SUMO-specific isopeptidase USPL1
Ligandability
Cysteine 226 of SUMO-specific isopeptidase USPL1
Cysteine 471 of SUMO-specific isopeptidase USPL1
7p99 A 226 A 478
A redox-regulated disulphide may form within SUMO-specific isopeptidase USPL1 between cysteines 226 and 478. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
7p99
Structure name
structure of human uspl1 in complex with sumo2
Structure deposition date
2021-07-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
3
% buried
54
Peptide accession
Q5W0Q7
Residue number A
226
Residue number B
478
Peptide name
SUMO-specific isopeptidase USPL1
Ligandability
Cysteine 226 of SUMO-specific isopeptidase USPL1
Cysteine 478 of SUMO-specific isopeptidase USPL1
7p99 A 236 A 240
A redox-regulated disulphide may form within SUMO-specific isopeptidase USPL1 between cysteines 236 and 240. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
7p99
Structure name
structure of human uspl1 in complex with sumo2
Structure deposition date
2021-07-26
Thiol separation (Å)
6
Half-sphere exposure sum ?
89
Minimum pKa ?
14
% buried
93
Peptide accession
Q5W0Q7
Residue number A
236
Residue number B
240
Peptide name
SUMO-specific isopeptidase USPL1
Ligandability
Cysteine 236 of SUMO-specific isopeptidase USPL1
Cysteine 240 of SUMO-specific isopeptidase USPL1
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