Dual specificity protein phosphatase 16
Intermolecular
Cysteine 81 and cysteine 81
Cysteine 50 and cysteine 50
Intramolecular
Cysteine 131 and cysteine 136
Cysteine 50 and cysteine 102
2vsw A 81 B 81
A redox-regulated disulphide may form between two units of Dual specificity protein phosphatase 16 at cysteines 81 and 81.
Details
Redox score ?
75
PDB code
2vsw
Structure name
the structure of the rhodanese domain of the human dual specificity phosphatase 16
Structure deposition date
2008-04-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
8
% buried
56
Peptide A name
Dual specificity protein phosphatase 16
Peptide B name
Dual specificity protein phosphatase 16
Peptide A accession
Q9BY84
Peptide B accession
Q9BY84
Peptide A residue number
81
Peptide B residue number
81
Ligandability
3tg3 B 50 C 50
A redox-regulated disulphide may form between two units of Dual specificity protein phosphatase 16 at cysteines 50 and 50. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
3tg3
Structure name
crystal structure of the mapk binding domain of mkp7
Structure deposition date
2011-08-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
78
Minimum pKa ?
14
% buried
100
Peptide A name
Dual specificity protein phosphatase 16
Peptide B name
Dual specificity protein phosphatase 16
Peptide A accession
Q9BY84
Peptide B accession
Q9BY84
Peptide A residue number
50
Peptide B residue number
50
Ligandability
2vsw A 131 A 136
A redox-regulated disulphide may form within Dual specificity protein phosphatase 16 between cysteines 131 and 136. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
2vsw
Structure name
the structure of the rhodanese domain of the human dual specificity phosphatase 16
Structure deposition date
2008-04-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
42
Minimum pKa ?
9
% buried
14
Peptide accession
Q9BY84
Residue number A
131
Residue number B
136
Peptide name
Dual specificity protein phosphatase 16
Ligandability
Cysteine 131 of Dual specificity protein phosphatase 16
Cysteine 136 of Dual specificity protein phosphatase 16
3tg3 A 50 A 102
A redox-regulated disulphide may form within Dual specificity protein phosphatase 16 between cysteines 50 and 102. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
3tg3
Structure name
crystal structure of the mapk binding domain of mkp7
Structure deposition date
2011-08-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
11
% buried
96
Peptide accession
Q9BY84
Residue number A
50
Residue number B
102
Peptide name
Dual specificity protein phosphatase 16
Ligandability
Cysteine 50 of Dual specificity protein phosphatase 16
Cysteine 102 of Dual specificity protein phosphatase 16
If this tool was useful for finding a disulphide, please cite: