Dual adapter for phosphotyrosine and 3-phosphotyrosine and 3-phosphoinositide
Intramolecular
Cysteine 227 and cysteine 240
Cysteine 213 and cysteine 229
Cysteine 227 and cysteine 229
Cysteine 229 and cysteine 240
1fao A 227 A 240
A redox-regulated disulphide may form within Dual adapter for phosphotyrosine and 3-phosphotyrosine and 3-phosphoinositide between cysteines 227 and 240.
Details
Redox score ?
78
PDB code
1fao
Structure name
structure of the pleckstrin homology domain from dapp1/phish in complex with inositol 1,3,4,5- tetrakisphosphate
Structure deposition date
2000-07-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UN19
Residue number A
227
Residue number B
240
Peptide name
Dual adapter for phosphotyrosine and 3-phosphotyrosine and 3-phosphoinositide
Ligandability
Cysteine 227 of Dual adapter for phosphotyrosine and 3-phosphotyrosine and 3-phosphoinositide
Cysteine 240 of Dual adapter for phosphotyrosine and 3-phosphotyrosine and 3-phosphoinositide
1fao A 213 A 229
A redox-regulated disulphide may form within Dual adapter for phosphotyrosine and 3-phosphotyrosine and 3-phosphoinositide between cysteines 213 and 229. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
1fao
Structure name
structure of the pleckstrin homology domain from dapp1/phish in complex with inositol 1,3,4,5- tetrakisphosphate
Structure deposition date
2000-07-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
45
Peptide accession
Q9UN19
Residue number A
213
Residue number B
229
Peptide name
Dual adapter for phosphotyrosine and 3-phosphotyrosine and 3-phosphoinositide
Ligandability
Cysteine 213 of Dual adapter for phosphotyrosine and 3-phosphotyrosine and 3-phosphoinositide
Cysteine 229 of Dual adapter for phosphotyrosine and 3-phosphotyrosine and 3-phosphoinositide
1fao A 227 A 229
A redox-regulated disulphide may form within Dual adapter for phosphotyrosine and 3-phosphotyrosine and 3-phosphoinositide between cysteines 227 and 229. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
1fao
Structure name
structure of the pleckstrin homology domain from dapp1/phish in complex with inositol 1,3,4,5- tetrakisphosphate
Structure deposition date
2000-07-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
nan
Peptide accession
Q9UN19
Residue number A
227
Residue number B
229
Peptide name
Dual adapter for phosphotyrosine and 3-phosphotyrosine and 3-phosphoinositide
Ligandability
Cysteine 227 of Dual adapter for phosphotyrosine and 3-phosphotyrosine and 3-phosphoinositide
Cysteine 229 of Dual adapter for phosphotyrosine and 3-phosphotyrosine and 3-phosphoinositide
1fao A 229 A 240
A redox-regulated disulphide may form within Dual adapter for phosphotyrosine and 3-phosphotyrosine and 3-phosphoinositide between cysteines 229 and 240. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
1fao
Structure name
structure of the pleckstrin homology domain from dapp1/phish in complex with inositol 1,3,4,5- tetrakisphosphate
Structure deposition date
2000-07-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
nan
Peptide accession
Q9UN19
Residue number A
229
Residue number B
240
Peptide name
Dual adapter for phosphotyrosine and 3-phosphotyrosine and 3-phosphoinositide
Ligandability
Cysteine 229 of Dual adapter for phosphotyrosine and 3-phosphotyrosine and 3-phosphoinositide
Cysteine 240 of Dual adapter for phosphotyrosine and 3-phosphotyrosine and 3-phosphoinositide
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