Pleiotrophin
Intramolecular
Cysteine 62 and cysteine 89
Cysteine 99 and cysteine 131
Cysteine 55 and cysteine 85
Cysteine 109 and cysteine 141
Cysteine 47 and cysteine 76
Cysteine 55 and cysteine 89
2n6f A 30 A 57
A redox-regulated disulphide may form within Pleiotrophin between cysteines 62 and 89 (30 and 57 respectively in this structure).
Details
Redox score ?
89
PDB code
2n6f
Structure name
structure of pleiotrophin
Structure deposition date
2015-08-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
31
Minimum pKa ?
nan
% buried
nan
Peptide accession
P21246
Residue number A
62
Residue number B
89
Peptide name
Pleiotrophin
Ligandability
Cysteine 62 of Pleiotrophin
Cysteine 89 of Pleiotrophin
2n6f A 67 A 99
A redox-regulated disulphide may form within Pleiotrophin between cysteines 99 and 131 (67 and 99 respectively in this structure).
Details
Redox score ?
89
PDB code
2n6f
Structure name
structure of pleiotrophin
Structure deposition date
2015-08-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
P21246
Residue number A
99
Residue number B
131
Peptide name
Pleiotrophin
Ligandability
Cysteine 99 of Pleiotrophin
Cysteine 131 of Pleiotrophin
2n6f A 23 A 53
A redox-regulated disulphide may form within Pleiotrophin between cysteines 55 and 85 (23 and 53 respectively in this structure).
Details
Redox score ?
88
PDB code
2n6f
Structure name
structure of pleiotrophin
Structure deposition date
2015-08-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
38
Minimum pKa ?
nan
% buried
nan
Peptide accession
P21246
Residue number A
55
Residue number B
85
Peptide name
Pleiotrophin
Ligandability
Cysteine 55 of Pleiotrophin
Cysteine 85 of Pleiotrophin
2n6f A 77 A 109
A redox-regulated disulphide may form within Pleiotrophin between cysteines 109 and 141 (77 and 109 respectively in this structure).
Details
Redox score ?
88
PDB code
2n6f
Structure name
structure of pleiotrophin
Structure deposition date
2015-08-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
36
Minimum pKa ?
nan
% buried
nan
Peptide accession
P21246
Residue number A
109
Residue number B
141
Peptide name
Pleiotrophin
Ligandability
Cysteine 109 of Pleiotrophin
Cysteine 141 of Pleiotrophin
2n6f A 15 A 44
A redox-regulated disulphide may form within Pleiotrophin between cysteines 47 and 76 (15 and 44 respectively in this structure).
Details
Redox score ?
87
PDB code
2n6f
Structure name
structure of pleiotrophin
Structure deposition date
2015-08-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
33
Minimum pKa ?
nan
% buried
nan
Peptide accession
P21246
Residue number A
47
Residue number B
76
Peptide name
Pleiotrophin
Ligandability
Cysteine 47 of Pleiotrophin
Cysteine 76 of Pleiotrophin
2n6f A 23 A 57
A redox-regulated disulphide may form within Pleiotrophin between cysteines 55 and 89 (23 and 57 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
2n6f
Structure name
structure of pleiotrophin
Structure deposition date
2015-08-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
34
Minimum pKa ?
nan
% buried
nan
Peptide accession
P21246
Residue number A
55
Residue number B
89
Peptide name
Pleiotrophin
Ligandability
Cysteine 55 of Pleiotrophin
Cysteine 89 of Pleiotrophin
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