ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Synaptotagmin-13

Intramolecular
Cysteine 191 and cysteine 193
Cysteine 191 and cysteine 246
Cysteine 193 and cysteine 246
A redox-regulated disulphide may form within Synaptotagmin-13 between cysteines 191 and 193 (44 and 46 respectively in this structure).

Details

Redox score ?
64
PDB code
1wfm
Structure name
the first c2 domain of human synaptotagmin xiii
Structure deposition date
2004-05-26
Thiol separation (Å)
6
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
26
Peptide accession
Q7L8C5
Residue number A
191
Residue number B
193
Peptide name
Synaptotagmin-13

Ligandability

Cysteine 191 of Synaptotagmin-13

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 193 of Synaptotagmin-13

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Synaptotagmin-13 between cysteines 191 and 246 (44 and 99 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
1wfm
Structure name
the first c2 domain of human synaptotagmin xiii
Structure deposition date
2004-05-26
Thiol separation (Å)
8
Half-sphere exposure sum ?
45
Minimum pKa ?
10
% buried
0
Peptide accession
Q7L8C5
Residue number A
191
Residue number B
246
Peptide name
Synaptotagmin-13

Ligandability

Cysteine 191 of Synaptotagmin-13

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 246 of Synaptotagmin-13

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Synaptotagmin-13 between cysteines 193 and 246 (46 and 99 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
1wfm
Structure name
the first c2 domain of human synaptotagmin xiii
Structure deposition date
2004-05-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
25
Peptide accession
Q7L8C5
Residue number A
193
Residue number B
246
Peptide name
Synaptotagmin-13

Ligandability

Cysteine 193 of Synaptotagmin-13

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 246 of Synaptotagmin-13

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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