ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Synapsin-2

Intermolecular
Cysteine 224 and cysteine 224
Intramolecular
Cysteine 361 and cysteine 371
Cysteine 371 and cysteine 391
Cysteine 224 and cysteine 391
A redox-regulated disulphide may form between two units of Synapsin-2 at cysteines 224 and 224. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
1i7n
Structure name
crystal structure analysis of the c domain of synapsin ii from rat brain
Structure deposition date
2001-03-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
13
% buried
100
Peptide A name
Synapsin-2
Peptide B name
Synapsin-2
Peptide A accession
Q63537
Peptide B accession
Q63537
Peptide A residue number
224
Peptide B residue number
224

Ligandability

A redox-regulated disulphide may form within Synapsin-2 between cysteines 361 and 371. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
1i7l
Structure name
crystal structure analysis of the complex of the c domain of synapsin ii from rat with atp
Structure deposition date
2001-03-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
85
Minimum pKa ?
12
% buried
100
Peptide accession
Q63537
Residue number A
361
Residue number B
371
Peptide name
Synapsin-2

Ligandability

Cysteine 361 of Synapsin-2

Cysteine 371 of Synapsin-2

A redox-regulated disulphide may form within Synapsin-2 between cysteines 371 and 391. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
1i7l
Structure name
crystal structure analysis of the complex of the c domain of synapsin ii from rat with atp
Structure deposition date
2001-03-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
100
Peptide accession
Q63537
Residue number A
371
Residue number B
391
Peptide name
Synapsin-2

Ligandability

Cysteine 371 of Synapsin-2

Cysteine 391 of Synapsin-2

A redox-regulated disulphide may form within Synapsin-2 between cysteines 224 and 391. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
1i7l
Structure name
crystal structure analysis of the complex of the c domain of synapsin ii from rat with atp
Structure deposition date
2001-03-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
13
% buried
100
Peptide accession
Q63537
Residue number A
224
Residue number B
391
Peptide name
Synapsin-2

Ligandability

Cysteine 224 of Synapsin-2

Cysteine 391 of Synapsin-2

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