Ubiquitin carboxyl-terminal hydrolase CYLD
Intramolecular
Cysteine 788 and cysteine 791
Cysteine 788 and cysteine 817
Cysteine 510 and cysteine 513
Cysteine 788 and cysteine 820
Cysteine 791 and cysteine 817
Cysteine 817 and cysteine 820
Cysteine 791 and cysteine 820
Cysteine 799 and cysteine 802
Cysteine 909 and cysteine 934
Cysteine 189 and cysteine 193
More...Cysteine 513 and cysteine 526
Cysteine 252 and cysteine 286
Cysteine 286 and cysteine 290
Cysteine 866 and cysteine 945
Cysteine 866 and cysteine 909
Cysteine 866 and cysteine 940
Cysteine 609 and cysteine 866
Cysteine 609 and cysteine 945
Cysteine 609 and cysteine 751
2vhf A 788 A 791
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase CYLD between cysteines 788 and 791.
Details
Redox score ?
84
PDB code
2vhf
Structure name
structure of the cyld usp domain
Structure deposition date
2007-11-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
6
% buried
11
Peptide accession
Q9NQC7
Residue number A
788
Residue number B
791
Peptide name
Ubiquitin carboxyl-terminal hydrolase CYLD
Ligandability
Cysteine 788 of Ubiquitin carboxyl-terminal hydrolase CYLD
Cysteine 791 of Ubiquitin carboxyl-terminal hydrolase CYLD
2vhf A 788 A 817
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase CYLD between cysteines 788 and 817.
Details
Redox score ?
83
PDB code
2vhf
Structure name
structure of the cyld usp domain
Structure deposition date
2007-11-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
6
% buried
12
Peptide accession
Q9NQC7
Residue number A
788
Residue number B
817
Peptide name
Ubiquitin carboxyl-terminal hydrolase CYLD
Ligandability
Cysteine 788 of Ubiquitin carboxyl-terminal hydrolase CYLD
Cysteine 817 of Ubiquitin carboxyl-terminal hydrolase CYLD
7owd B 510 B 513
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase CYLD between cysteines 510 and 513.
Details
Redox score ?
82
PDB code
7owd
Structure name
structure of cyld cap-gly3 (467-552) bound to ub; tetragonal space group
Structure deposition date
2021-06-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
8
% buried
10
Peptide accession
Q9NQC7
Residue number A
510
Residue number B
513
Peptide name
Ubiquitin carboxyl-terminal hydrolase CYLD
Ligandability
Cysteine 510 of Ubiquitin carboxyl-terminal hydrolase CYLD
Cysteine 513 of Ubiquitin carboxyl-terminal hydrolase CYLD
2vhf B 788 B 820
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase CYLD between cysteines 788 and 820.
Details
Redox score ?
78
PDB code
2vhf
Structure name
structure of the cyld usp domain
Structure deposition date
2007-11-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
8
% buried
38
Peptide accession
Q9NQC7
Residue number A
788
Residue number B
820
Peptide name
Ubiquitin carboxyl-terminal hydrolase CYLD
Ligandability
Cysteine 788 of Ubiquitin carboxyl-terminal hydrolase CYLD
Cysteine 820 of Ubiquitin carboxyl-terminal hydrolase CYLD
2vhf A 791 A 817
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase CYLD between cysteines 791 and 817.
Details
Redox score ?
76
PDB code
2vhf
Structure name
structure of the cyld usp domain
Structure deposition date
2007-11-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
8
% buried
0
Peptide accession
Q9NQC7
Residue number A
791
Residue number B
817
Peptide name
Ubiquitin carboxyl-terminal hydrolase CYLD
Ligandability
Cysteine 791 of Ubiquitin carboxyl-terminal hydrolase CYLD
Cysteine 817 of Ubiquitin carboxyl-terminal hydrolase CYLD
2vhf A 817 A 820
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase CYLD between cysteines 817 and 820.
Details
Redox score ?
75
PDB code
2vhf
Structure name
structure of the cyld usp domain
Structure deposition date
2007-11-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
8
% buried
2
Peptide accession
Q9NQC7
Residue number A
817
Residue number B
820
Peptide name
Ubiquitin carboxyl-terminal hydrolase CYLD
Ligandability
Cysteine 817 of Ubiquitin carboxyl-terminal hydrolase CYLD
Cysteine 820 of Ubiquitin carboxyl-terminal hydrolase CYLD
2vhf A 791 A 820
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase CYLD between cysteines 791 and 820.
Details
Redox score ?
74
PDB code
2vhf
Structure name
structure of the cyld usp domain
Structure deposition date
2007-11-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
9
% buried
2
Peptide accession
Q9NQC7
Residue number A
791
Residue number B
820
Peptide name
Ubiquitin carboxyl-terminal hydrolase CYLD
Ligandability
Cysteine 791 of Ubiquitin carboxyl-terminal hydrolase CYLD
Cysteine 820 of Ubiquitin carboxyl-terminal hydrolase CYLD
2vhf B 799 B 802
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase CYLD between cysteines 799 and 802.
Details
Redox score ?
71
PDB code
2vhf
Structure name
structure of the cyld usp domain
Structure deposition date
2007-11-21
Thiol separation (Å)
5
Half-sphere exposure sum ?
66
Minimum pKa ?
9
% buried
46
Peptide accession
Q9NQC7
Residue number A
799
Residue number B
802
Peptide name
Ubiquitin carboxyl-terminal hydrolase CYLD
Ligandability
Cysteine 799 of Ubiquitin carboxyl-terminal hydrolase CYLD
Cysteine 802 of Ubiquitin carboxyl-terminal hydrolase CYLD
2vhf A 909 A 934
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase CYLD between cysteines 909 and 934.
Details
Redox score ?
66
PDB code
2vhf
Structure name
structure of the cyld usp domain
Structure deposition date
2007-11-21
Thiol separation (Å)
5
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
47
Peptide accession
Q9NQC7
Residue number A
909
Residue number B
934
Peptide name
Ubiquitin carboxyl-terminal hydrolase CYLD
Ligandability
Cysteine 909 of Ubiquitin carboxyl-terminal hydrolase CYLD
Cysteine 934 of Ubiquitin carboxyl-terminal hydrolase CYLD
1whl A 72 A 76
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase CYLD between cysteines 189 and 193 (72 and 76 respectively in this structure).
Details
Redox score ?
63
PDB code
1whl
Structure name
solution structure of the 1st cap-gly domain in human cylindromatosis tumor suppressor cyld
Structure deposition date
2004-05-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
19
Peptide accession
Q9NQC7
Residue number A
189
Residue number B
193
Peptide name
Ubiquitin carboxyl-terminal hydrolase CYLD
Ligandability
Cysteine 189 of Ubiquitin carboxyl-terminal hydrolase CYLD
Cysteine 193 of Ubiquitin carboxyl-terminal hydrolase CYLD
7owd B 513 B 526
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase CYLD between cysteines 513 and 526. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
7owd
Structure name
structure of cyld cap-gly3 (467-552) bound to ub; tetragonal space group
Structure deposition date
2021-06-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
52
Minimum pKa ?
11
% buried
24
Peptide accession
Q9NQC7
Residue number A
513
Residue number B
526
Peptide name
Ubiquitin carboxyl-terminal hydrolase CYLD
Ligandability
Cysteine 513 of Ubiquitin carboxyl-terminal hydrolase CYLD
Cysteine 526 of Ubiquitin carboxyl-terminal hydrolase CYLD
1whm A 32 A 66
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase CYLD between cysteines 252 and 286 (32 and 66 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
1whm
Structure name
solution structure of the 2nd cap-gly domain in human cylindromatosis tumor suppressor cyld
Structure deposition date
2004-05-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
34
Peptide accession
Q9NQC7
Residue number A
252
Residue number B
286
Peptide name
Ubiquitin carboxyl-terminal hydrolase CYLD
Ligandability
Cysteine 252 of Ubiquitin carboxyl-terminal hydrolase CYLD
Cysteine 286 of Ubiquitin carboxyl-terminal hydrolase CYLD
1whm A 66 A 70
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase CYLD between cysteines 286 and 290 (66 and 70 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
1whm
Structure name
solution structure of the 2nd cap-gly domain in human cylindromatosis tumor suppressor cyld
Structure deposition date
2004-05-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
16
Peptide accession
Q9NQC7
Residue number A
286
Residue number B
290
Peptide name
Ubiquitin carboxyl-terminal hydrolase CYLD
Ligandability
Cysteine 286 of Ubiquitin carboxyl-terminal hydrolase CYLD
Cysteine 290 of Ubiquitin carboxyl-terminal hydrolase CYLD
2vhf A 866 A 945
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase CYLD between cysteines 866 and 945. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
2vhf
Structure name
structure of the cyld usp domain
Structure deposition date
2007-11-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
87
Minimum pKa ?
13
% buried
100
Peptide accession
Q9NQC7
Residue number A
866
Residue number B
945
Peptide name
Ubiquitin carboxyl-terminal hydrolase CYLD
Ligandability
Cysteine 866 of Ubiquitin carboxyl-terminal hydrolase CYLD
Cysteine 945 of Ubiquitin carboxyl-terminal hydrolase CYLD
2vhf A 866 A 909
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase CYLD between cysteines 866 and 909. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
2vhf
Structure name
structure of the cyld usp domain
Structure deposition date
2007-11-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
84
Peptide accession
Q9NQC7
Residue number A
866
Residue number B
909
Peptide name
Ubiquitin carboxyl-terminal hydrolase CYLD
Ligandability
Cysteine 866 of Ubiquitin carboxyl-terminal hydrolase CYLD
Cysteine 909 of Ubiquitin carboxyl-terminal hydrolase CYLD
2vhf A 866 A 940
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase CYLD between cysteines 866 and 940. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
2vhf
Structure name
structure of the cyld usp domain
Structure deposition date
2007-11-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
11
% buried
74
Peptide accession
Q9NQC7
Residue number A
866
Residue number B
940
Peptide name
Ubiquitin carboxyl-terminal hydrolase CYLD
Ligandability
Cysteine 866 of Ubiquitin carboxyl-terminal hydrolase CYLD
Cysteine 940 of Ubiquitin carboxyl-terminal hydrolase CYLD
2vhf A 609 A 866
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase CYLD between cysteines 609 and 866. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
2vhf
Structure name
structure of the cyld usp domain
Structure deposition date
2007-11-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
87
Minimum pKa ?
13
% buried
100
Peptide accession
Q9NQC7
Residue number A
609
Residue number B
866
Peptide name
Ubiquitin carboxyl-terminal hydrolase CYLD
Ligandability
Cysteine 609 of Ubiquitin carboxyl-terminal hydrolase CYLD
Cysteine 866 of Ubiquitin carboxyl-terminal hydrolase CYLD
2vhf B 609 B 945
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase CYLD between cysteines 609 and 945. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
25
PDB code
2vhf
Structure name
structure of the cyld usp domain
Structure deposition date
2007-11-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
92
Minimum pKa ?
13
% buried
100
Peptide accession
Q9NQC7
Residue number A
609
Residue number B
945
Peptide name
Ubiquitin carboxyl-terminal hydrolase CYLD
Ligandability
Cysteine 609 of Ubiquitin carboxyl-terminal hydrolase CYLD
Cysteine 945 of Ubiquitin carboxyl-terminal hydrolase CYLD
2vhf A 609 A 751
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase CYLD between cysteines 609 and 751. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
24
PDB code
2vhf
Structure name
structure of the cyld usp domain
Structure deposition date
2007-11-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
100
Peptide accession
Q9NQC7
Residue number A
609
Residue number B
751
Peptide name
Ubiquitin carboxyl-terminal hydrolase CYLD
Ligandability
Cysteine 609 of Ubiquitin carboxyl-terminal hydrolase CYLD
Cysteine 751 of Ubiquitin carboxyl-terminal hydrolase CYLD
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