ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Tyrosine-protein kinase Fyn

Intramolecular
Cysteine 239 and cysteine 240
Cysteine 487 and cysteine 491
A redox-regulated disulphide may form within Tyrosine-protein kinase Fyn between cysteines 239 and 240 (103 and 104 respectively in this structure).

Details

Redox score ?
81
PDB code
4u17
Structure name
swapped dimer of the human fyn-sh2 domain
Structure deposition date
2014-07-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
22
Minimum pKa ?
8
% buried
0
Peptide accession
P06241
Residue number A
239
Residue number B
240
Peptide name
Tyrosine-protein kinase Fyn

Ligandability

Cysteine 239 of Tyrosine-protein kinase Fyn

Cysteine 240 of Tyrosine-protein kinase Fyn

A redox-regulated disulphide may form within Tyrosine-protein kinase Fyn between cysteines 487 and 491 (227 and 231 respectively in this structure).

Details

Redox score ?
76
PDB code
2dq7
Structure name
crystal structure of fyn kinase domain complexed with staurosporine
Structure deposition date
2006-05-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
9
% buried
22
Peptide accession
P06241
Residue number A
487
Residue number B
491
Peptide name
Tyrosine-protein kinase Fyn

Ligandability

Cysteine 487 of Tyrosine-protein kinase Fyn

Cysteine 491 of Tyrosine-protein kinase Fyn

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