Protein numb homolog
Intermolecular
Cysteine 160 and cysteine 160
Intramolecular
Cysteine 141 and cysteine 143
Cysteine 58 and cysteine 141
Cysteine 58 and cysteine 143
Cysteine 131 and cysteine 141
Cysteine 37 and cysteine 160
Cysteine 58 and cysteine 117 L
Cysteine 117 and cysteine 141 L
Cysteine 131 and cysteine 143
Cysteine 117 and cysteine 160 L
5njj B 160 D 160
A redox-regulated disulphide may form between two units of Protein numb homolog at cysteines 160 and 160. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
5njj
Structure name
ptb domain of human numb isoform-1
Structure deposition date
2017-03-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
93
Minimum pKa ?
12
% buried
92
Peptide A name
Protein numb homolog
Peptide B name
Protein numb homolog
Peptide A accession
P49757
Peptide B accession
P49757
Peptide A residue number
160
Peptide B residue number
160
Ligandability
5njk D 141 D 143
A redox-regulated disulphide may form within Protein numb homolog between cysteines 141 and 143.
Details
Redox score ?
67
PDB code
5njk
Structure name
ptb domain of human numb isoform-1
Structure deposition date
2017-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
83
Minimum pKa ?
10
% buried
100
Peptide accession
P49757
Residue number A
141
Residue number B
143
Peptide name
Protein numb homolog
Ligandability
Cysteine 141 of Protein numb homolog
Cysteine 143 of Protein numb homolog
5njj A 58 A 141
A redox-regulated disulphide may form within Protein numb homolog between cysteines 58 and 141. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
5njj
Structure name
ptb domain of human numb isoform-1
Structure deposition date
2017-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
82
Minimum pKa ?
14
% buried
98
Peptide accession
P49757
Residue number A
58
Residue number B
141
Peptide name
Protein numb homolog
Ligandability
Cysteine 58 of Protein numb homolog
Cysteine 141 of Protein numb homolog
5njj D 58 D 143
A redox-regulated disulphide may form within Protein numb homolog between cysteines 58 and 143. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
5njj
Structure name
ptb domain of human numb isoform-1
Structure deposition date
2017-03-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
82
Minimum pKa ?
8
% buried
90
Peptide accession
P49757
Residue number A
58
Residue number B
143
Peptide name
Protein numb homolog
Ligandability
Cysteine 58 of Protein numb homolog
Cysteine 143 of Protein numb homolog
1wj1 A 109 A 119
A redox-regulated disulphide may form within Protein numb homolog between cysteines 131 and 141 (109 and 119 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
1wj1
Structure name
solution structure of phosphotyrosine interaction domain of mouse numb protein
Structure deposition date
2004-05-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
76
Peptide accession
Q9QZS3
Residue number A
131
Residue number B
141
Peptide name
Protein numb homolog
Ligandability
Cysteine 131 of Protein numb homolog
Cysteine 141 of Protein numb homolog
1wj1 A 26 A 138
A redox-regulated disulphide may form within Protein numb homolog between cysteines 37 and 160 (26 and 138 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
1wj1
Structure name
solution structure of phosphotyrosine interaction domain of mouse numb protein
Structure deposition date
2004-05-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
77
Minimum pKa ?
13
% buried
65
Peptide accession
Q9QZS3
Residue number A
37
Residue number B
160
Peptide name
Protein numb homolog
Ligandability
Cysteine 37 of Protein numb homolog
Cysteine 160 of Protein numb homolog
1wj1 A 47 A 95
A redox-regulated disulphide may form within Protein numb homolog between cysteines 58 and 117 (47 and 95 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
1wj1
Structure name
solution structure of phosphotyrosine interaction domain of mouse numb protein
Structure deposition date
2004-05-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
82
Minimum pKa ?
11
% buried
76
Peptide accession
Q9QZS3
Residue number A
58
Residue number B
117
Peptide name
Protein numb homolog
Ligandability
Cysteine 58 of Protein numb homolog
Cysteine 117 of Protein numb homolog
1wj1 A 95 A 119
A redox-regulated disulphide may form within Protein numb homolog between cysteines 117 and 141 (95 and 119 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
1wj1
Structure name
solution structure of phosphotyrosine interaction domain of mouse numb protein
Structure deposition date
2004-05-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
83
Minimum pKa ?
11
% buried
82
Peptide accession
Q9QZS3
Residue number A
117
Residue number B
141
Peptide name
Protein numb homolog
Ligandability
Cysteine 117 of Protein numb homolog
Cysteine 141 of Protein numb homolog
1wj1 A 109 A 121
A redox-regulated disulphide may form within Protein numb homolog between cysteines 131 and 143 (109 and 121 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
1wj1
Structure name
solution structure of phosphotyrosine interaction domain of mouse numb protein
Structure deposition date
2004-05-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
11
% buried
79
Peptide accession
Q9QZS3
Residue number A
131
Residue number B
143
Peptide name
Protein numb homolog
Ligandability
Cysteine 131 of Protein numb homolog
Cysteine 143 of Protein numb homolog
1wj1 A 95 A 138
A redox-regulated disulphide may form within Protein numb homolog between cysteines 117 and 160 (95 and 138 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
1wj1
Structure name
solution structure of phosphotyrosine interaction domain of mouse numb protein
Structure deposition date
2004-05-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
11
% buried
70
Peptide accession
Q9QZS3
Residue number A
117
Residue number B
160
Peptide name
Protein numb homolog
Ligandability
Cysteine 117 of Protein numb homolog
Cysteine 160 of Protein numb homolog
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