ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Ubiquitin carboxyl-terminal hydrolase 2

Intermolecular
Cysteine 485 and cysteine 2 of Polyubiquitin-B
Intramolecular
Cysteine 425 and cysteine 479
Cysteine 425 and cysteine 476
Cysteine 476 and cysteine 479
Cysteine 425 and cysteine 428
Cysteine 428 and cysteine 476
Cysteine 428 and cysteine 479
Cysteine 425 and cysteine 485
Cysteine 476 and cysteine 485
Cysteine 476 and cysteine 477
More...
Cysteine 284 and cysteine 562
Cysteine 428 and cysteine 485
Cysteine 479 and cysteine 485
Cysteine 477 and cysteine 479
Cysteine 425 and cysteine 477
Cysteine 477 and cysteine 485
Cysteine 431 and cysteine 485
Cysteine 428 and cysteine 477
A redox-regulated disulphide may form between cysteine 485 of Ubiquitin carboxyl-terminal hydrolase 2 and cysteine 2 of Polyubiquitin-B.

Details

Redox score ?
nan
PDB code
6dgf
Structure name
ubiquitin variant bound to usp2
Structure deposition date
2018-05-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
44
Peptide A name
Ubiquitin carboxyl-terminal hydrolase 2
Peptide B name
Polyubiquitin-B
Peptide A accession
O75604
Peptide B accession
P0CG47
Peptide A residue number
485
Peptide B residue number
2

Ligandability

Cysteine 485 of Ubiquitin carboxyl-terminal hydrolase 2

Cysteine 2 of Polyubiquitin-B

Cysteine 2 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 2 between cysteines 425 and 479.

Details

Redox score ?
87
PDB code
3nhe
Structure name
high resolution structure (1
Structure deposition date
2010-06-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
6
% buried
0
Peptide accession
O75604
Residue number A
425
Residue number B
479
Peptide name
Ubiquitin carboxyl-terminal hydrolase 2

Ligandability

Cysteine 425 of Ubiquitin carboxyl-terminal hydrolase 2

Cysteine 479 of Ubiquitin carboxyl-terminal hydrolase 2

A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 2 between cysteines 425 and 476.

Details

Redox score ?
87
PDB code
6dgf
Structure name
ubiquitin variant bound to usp2
Structure deposition date
2018-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
6
% buried
0
Peptide accession
O75604
Residue number A
425
Residue number B
476
Peptide name
Ubiquitin carboxyl-terminal hydrolase 2

Ligandability

Cysteine 425 of Ubiquitin carboxyl-terminal hydrolase 2

Cysteine 476 of Ubiquitin carboxyl-terminal hydrolase 2

A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 2 between cysteines 476 and 479.

Details

Redox score ?
84
PDB code
6dgf
Structure name
ubiquitin variant bound to usp2
Structure deposition date
2018-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
8
% buried
0
Peptide accession
O75604
Residue number A
476
Residue number B
479
Peptide name
Ubiquitin carboxyl-terminal hydrolase 2

Ligandability

Cysteine 476 of Ubiquitin carboxyl-terminal hydrolase 2

Cysteine 479 of Ubiquitin carboxyl-terminal hydrolase 2

A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 2 between cysteines 425 and 428 (334 and 337 respectively in this structure).

Details

Redox score ?
84
PDB code
2hd5
Structure name
usp2 in complex with ubiquitin
Structure deposition date
2006-06-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
6
% buried
0
Peptide accession
O75604
Residue number A
425
Residue number B
428
Peptide name
Ubiquitin carboxyl-terminal hydrolase 2

Ligandability

Cysteine 425 of Ubiquitin carboxyl-terminal hydrolase 2

Cysteine 428 of Ubiquitin carboxyl-terminal hydrolase 2

A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 2 between cysteines 428 and 476.

Details

Redox score ?
83
PDB code
6dgf
Structure name
ubiquitin variant bound to usp2
Structure deposition date
2018-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
8
% buried
0
Peptide accession
O75604
Residue number A
428
Residue number B
476
Peptide name
Ubiquitin carboxyl-terminal hydrolase 2

Ligandability

Cysteine 428 of Ubiquitin carboxyl-terminal hydrolase 2

Cysteine 476 of Ubiquitin carboxyl-terminal hydrolase 2

A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 2 between cysteines 428 and 479 (337 and 384 respectively in this structure).

Details

Redox score ?
79
PDB code
2hd5
Structure name
usp2 in complex with ubiquitin
Structure deposition date
2006-06-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
9
% buried
0
Peptide accession
O75604
Residue number A
428
Residue number B
479
Peptide name
Ubiquitin carboxyl-terminal hydrolase 2

Ligandability

Cysteine 428 of Ubiquitin carboxyl-terminal hydrolase 2

Cysteine 479 of Ubiquitin carboxyl-terminal hydrolase 2

A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 2 between cysteines 425 and 485.

Details

Redox score ?
78
PDB code
3nhe
Structure name
high resolution structure (1
Structure deposition date
2010-06-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
65
Minimum pKa ?
6
% buried
20
Peptide accession
O75604
Residue number A
425
Residue number B
485
Peptide name
Ubiquitin carboxyl-terminal hydrolase 2

Ligandability

Cysteine 425 of Ubiquitin carboxyl-terminal hydrolase 2

Cysteine 485 of Ubiquitin carboxyl-terminal hydrolase 2

A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 2 between cysteines 476 and 485.

Details

Redox score ?
68
PDB code
2ibi
Structure name
covalent ubiquitin-usp2 complex
Structure deposition date
2006-09-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
63
Minimum pKa ?
7
% buried
20
Peptide accession
O75604
Residue number A
476
Residue number B
485
Peptide name
Ubiquitin carboxyl-terminal hydrolase 2

Ligandability

Cysteine 476 of Ubiquitin carboxyl-terminal hydrolase 2

Cysteine 485 of Ubiquitin carboxyl-terminal hydrolase 2

A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 2 between cysteines 476 and 477.

Details

Redox score ?
64
PDB code
2ibi
Structure name
covalent ubiquitin-usp2 complex
Structure deposition date
2006-09-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
51
Minimum pKa ?
7
% buried
12
Peptide accession
O75604
Residue number A
476
Residue number B
477
Peptide name
Ubiquitin carboxyl-terminal hydrolase 2

Ligandability

Cysteine 476 of Ubiquitin carboxyl-terminal hydrolase 2

Cysteine 477 of Ubiquitin carboxyl-terminal hydrolase 2

A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 2 between cysteines 284 and 562. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
3nhe
Structure name
high resolution structure (1
Structure deposition date
2010-06-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
92
Minimum pKa ?
12
% buried
100
Peptide accession
O75604
Residue number A
284
Residue number B
562
Peptide name
Ubiquitin carboxyl-terminal hydrolase 2

Ligandability

Cysteine 284 of Ubiquitin carboxyl-terminal hydrolase 2

Cysteine 562 of Ubiquitin carboxyl-terminal hydrolase 2

A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 2 between cysteines 428 and 485. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
3nhe
Structure name
high resolution structure (1
Structure deposition date
2010-06-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
20
Peptide accession
O75604
Residue number A
428
Residue number B
485
Peptide name
Ubiquitin carboxyl-terminal hydrolase 2

Ligandability

Cysteine 428 of Ubiquitin carboxyl-terminal hydrolase 2

Cysteine 485 of Ubiquitin carboxyl-terminal hydrolase 2

A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 2 between cysteines 479 and 485. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
2ibi
Structure name
covalent ubiquitin-usp2 complex
Structure deposition date
2006-09-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
52
Minimum pKa ?
11
% buried
19
Peptide accession
O75604
Residue number A
479
Residue number B
485
Peptide name
Ubiquitin carboxyl-terminal hydrolase 2

Ligandability

Cysteine 479 of Ubiquitin carboxyl-terminal hydrolase 2

Cysteine 485 of Ubiquitin carboxyl-terminal hydrolase 2

A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 2 between cysteines 477 and 479. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
3v6c
Structure name
crystal structure of usp2 in complex with mutated ubiquitin
Structure deposition date
2011-12-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75604
Residue number A
477
Residue number B
479
Peptide name
Ubiquitin carboxyl-terminal hydrolase 2

Ligandability

Cysteine 477 of Ubiquitin carboxyl-terminal hydrolase 2

Cysteine 479 of Ubiquitin carboxyl-terminal hydrolase 2

A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 2 between cysteines 425 and 477. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
3v6c
Structure name
crystal structure of usp2 in complex with mutated ubiquitin
Structure deposition date
2011-12-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75604
Residue number A
425
Residue number B
477
Peptide name
Ubiquitin carboxyl-terminal hydrolase 2

Ligandability

Cysteine 425 of Ubiquitin carboxyl-terminal hydrolase 2

Cysteine 477 of Ubiquitin carboxyl-terminal hydrolase 2

A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 2 between cysteines 477 and 485. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
6dgf
Structure name
ubiquitin variant bound to usp2
Structure deposition date
2018-05-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
21
Peptide accession
O75604
Residue number A
477
Residue number B
485
Peptide name
Ubiquitin carboxyl-terminal hydrolase 2

Ligandability

Cysteine 477 of Ubiquitin carboxyl-terminal hydrolase 2

Cysteine 485 of Ubiquitin carboxyl-terminal hydrolase 2

A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 2 between cysteines 431 and 485 (340 and 389 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
2hd5
Structure name
usp2 in complex with ubiquitin
Structure deposition date
2006-06-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
41
Peptide accession
O75604
Residue number A
431
Residue number B
485
Peptide name
Ubiquitin carboxyl-terminal hydrolase 2

Ligandability

Cysteine 431 of Ubiquitin carboxyl-terminal hydrolase 2

Cysteine 485 of Ubiquitin carboxyl-terminal hydrolase 2

A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 2 between cysteines 428 and 477. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2ibi
Structure name
covalent ubiquitin-usp2 complex
Structure deposition date
2006-09-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
43
Minimum pKa ?
9
% buried
10
Peptide accession
O75604
Residue number A
428
Residue number B
477
Peptide name
Ubiquitin carboxyl-terminal hydrolase 2

Ligandability

Cysteine 428 of Ubiquitin carboxyl-terminal hydrolase 2

Cysteine 477 of Ubiquitin carboxyl-terminal hydrolase 2

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