Ubiquitin carboxyl-terminal hydrolase 16
Intramolecular
Cysteine 48 and cysteine 82 L
Cysteine 51 and cysteine 82 L
Cysteine 24 and cysteine 119
Cysteine 116 and cysteine 119
Cysteine 24 and cysteine 116
Cysteine 48 and cysteine 51
Cysteine 74 and cysteine 77
Cysteine 104 and cysteine 116
Cysteine 24 and cysteine 104
Cysteine 104 and cysteine 119
Cysteine 74 and cysteine 104
2i50 A 31 A 65
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 16 between cysteines 48 and 82 (31 and 65 respectively in this structure).
Details
Redox score ?
87
PDB code
2i50
Structure name
solution structure of ubp-m znf-ubp domain
Structure deposition date
2006-08-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
2
% buried
58
Peptide accession
Q9Y5T5
Residue number A
48
Residue number B
82
Peptide name
Ubiquitin carboxyl-terminal hydrolase 16
Ligandability
Cysteine 48 of Ubiquitin carboxyl-terminal hydrolase 16
Cysteine 82 of Ubiquitin carboxyl-terminal hydrolase 16
2i50 A 34 A 65
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 16 between cysteines 51 and 82 (34 and 65 respectively in this structure).
Details
Redox score ?
87
PDB code
2i50
Structure name
solution structure of ubp-m znf-ubp domain
Structure deposition date
2006-08-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
2
% buried
47
Peptide accession
Q9Y5T5
Residue number A
51
Residue number B
82
Peptide name
Ubiquitin carboxyl-terminal hydrolase 16
Ligandability
Cysteine 51 of Ubiquitin carboxyl-terminal hydrolase 16
Cysteine 82 of Ubiquitin carboxyl-terminal hydrolase 16
2i50 A 7 A 102
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 16 between cysteines 24 and 119 (7 and 102 respectively in this structure).
Details
Redox score ?
80
PDB code
2i50
Structure name
solution structure of ubp-m znf-ubp domain
Structure deposition date
2006-08-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
9
% buried
18
Peptide accession
Q9Y5T5
Residue number A
24
Residue number B
119
Peptide name
Ubiquitin carboxyl-terminal hydrolase 16
Ligandability
Cysteine 24 of Ubiquitin carboxyl-terminal hydrolase 16
Cysteine 119 of Ubiquitin carboxyl-terminal hydrolase 16
2i50 A 99 A 102
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 16 between cysteines 116 and 119 (99 and 102 respectively in this structure).
Details
Redox score ?
77
PDB code
2i50
Structure name
solution structure of ubp-m znf-ubp domain
Structure deposition date
2006-08-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
9
% buried
24
Peptide accession
Q9Y5T5
Residue number A
116
Residue number B
119
Peptide name
Ubiquitin carboxyl-terminal hydrolase 16
Ligandability
Cysteine 116 of Ubiquitin carboxyl-terminal hydrolase 16
Cysteine 119 of Ubiquitin carboxyl-terminal hydrolase 16
2i50 A 7 A 99
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 16 between cysteines 24 and 116 (7 and 99 respectively in this structure).
Details
Redox score ?
74
PDB code
2i50
Structure name
solution structure of ubp-m znf-ubp domain
Structure deposition date
2006-08-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
38
Peptide accession
Q9Y5T5
Residue number A
24
Residue number B
116
Peptide name
Ubiquitin carboxyl-terminal hydrolase 16
Ligandability
Cysteine 24 of Ubiquitin carboxyl-terminal hydrolase 16
Cysteine 116 of Ubiquitin carboxyl-terminal hydrolase 16
2i50 A 31 A 34
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 16 between cysteines 48 and 51 (31 and 34 respectively in this structure).
Details
Redox score ?
72
PDB code
2i50
Structure name
solution structure of ubp-m znf-ubp domain
Structure deposition date
2006-08-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
52
Peptide accession
Q9Y5T5
Residue number A
48
Residue number B
51
Peptide name
Ubiquitin carboxyl-terminal hydrolase 16
Ligandability
Cysteine 48 of Ubiquitin carboxyl-terminal hydrolase 16
Cysteine 51 of Ubiquitin carboxyl-terminal hydrolase 16
2i50 A 57 A 60
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 16 between cysteines 74 and 77 (57 and 60 respectively in this structure).
Details
Redox score ?
72
PDB code
2i50
Structure name
solution structure of ubp-m znf-ubp domain
Structure deposition date
2006-08-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
82
Minimum pKa ?
6
% buried
88
Peptide accession
Q9Y5T5
Residue number A
74
Residue number B
77
Peptide name
Ubiquitin carboxyl-terminal hydrolase 16
Ligandability
Cysteine 74 of Ubiquitin carboxyl-terminal hydrolase 16
Cysteine 77 of Ubiquitin carboxyl-terminal hydrolase 16
2i50 A 87 A 99
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 16 between cysteines 104 and 116 (87 and 99 respectively in this structure).
Details
Redox score ?
69
PDB code
2i50
Structure name
solution structure of ubp-m znf-ubp domain
Structure deposition date
2006-08-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
79
Minimum pKa ?
9
% buried
48
Peptide accession
Q9Y5T5
Residue number A
104
Residue number B
116
Peptide name
Ubiquitin carboxyl-terminal hydrolase 16
Ligandability
Cysteine 104 of Ubiquitin carboxyl-terminal hydrolase 16
Cysteine 116 of Ubiquitin carboxyl-terminal hydrolase 16
2i50 A 7 A 87
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 16 between cysteines 24 and 104 (7 and 87 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
2i50
Structure name
solution structure of ubp-m znf-ubp domain
Structure deposition date
2006-08-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
71
Minimum pKa ?
9
% buried
42
Peptide accession
Q9Y5T5
Residue number A
24
Residue number B
104
Peptide name
Ubiquitin carboxyl-terminal hydrolase 16
Ligandability
Cysteine 24 of Ubiquitin carboxyl-terminal hydrolase 16
Cysteine 104 of Ubiquitin carboxyl-terminal hydrolase 16
2i50 A 87 A 102
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 16 between cysteines 104 and 119 (87 and 102 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
2i50
Structure name
solution structure of ubp-m znf-ubp domain
Structure deposition date
2006-08-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
9
% buried
28
Peptide accession
Q9Y5T5
Residue number A
104
Residue number B
119
Peptide name
Ubiquitin carboxyl-terminal hydrolase 16
Ligandability
Cysteine 104 of Ubiquitin carboxyl-terminal hydrolase 16
Cysteine 119 of Ubiquitin carboxyl-terminal hydrolase 16
2i50 A 57 A 87
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 16 between cysteines 74 and 104 (57 and 87 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
2i50
Structure name
solution structure of ubp-m znf-ubp domain
Structure deposition date
2006-08-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
91
Minimum pKa ?
6
% buried
74
Peptide accession
Q9Y5T5
Residue number A
74
Residue number B
104
Peptide name
Ubiquitin carboxyl-terminal hydrolase 16
Ligandability
Cysteine 74 of Ubiquitin carboxyl-terminal hydrolase 16
Cysteine 104 of Ubiquitin carboxyl-terminal hydrolase 16
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