ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Spermidine synthase

Intramolecular
Cysteine 224 and cysteine 251
Cysteine 205 and cysteine 224 L
Cysteine 204 and cysteine 205 L
Cysteine 205 and cysteine 251 L
Cysteine 204 and cysteine 251 L
Cysteine 204 and cysteine 236 L
A redox-regulated disulphide may form within Spermidine synthase between cysteines 224 and 251.

Details

Redox score ?
71
PDB code
3rw9
Structure name
crystal structure of human spermidine synthase in complex with decarboxylated s-adenosylhomocysteine
Structure deposition date
2011-05-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
79
Minimum pKa ?
8
% buried
84
Peptide accession
P19623
Residue number A
224
Residue number B
251
Peptide name
Spermidine synthase

Ligandability

Cysteine 224 of Spermidine synthase

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 251 of Spermidine synthase

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 Spermidine synthase between cysteines 205 and 224. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
2o0l
Structure name
human spermidine synthase
Structure deposition date
2006-11-27
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
8
% buried
86
Peptide accession
P19623
Residue number A
205
Residue number B
224
Peptide name
Spermidine synthase

Ligandability

Cysteine 205 of Spermidine synthase

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 224 of Spermidine synthase

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 Spermidine synthase between cysteines 204 and 205. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
2o05
Structure name
human spermidine synthase
Structure deposition date
2006-11-27
Thiol separation (Å)
7
Half-sphere exposure sum ?
92
Minimum pKa ?
12
% buried
100
Peptide accession
P19623
Residue number A
204
Residue number B
205
Peptide name
Spermidine synthase

Ligandability

Cysteine 204 of Spermidine synthase

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 205 of Spermidine synthase

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Spermidine synthase between cysteines 205 and 251. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
2o05
Structure name
human spermidine synthase
Structure deposition date
2006-11-27
Thiol separation (Å)
7
Half-sphere exposure sum ?
96
Minimum pKa ?
12
% buried
100
Peptide accession
P19623
Residue number A
205
Residue number B
251
Peptide name
Spermidine synthase

Ligandability

Cysteine 205 of Spermidine synthase

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 251 of Spermidine synthase

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 Spermidine synthase between cysteines 204 and 251. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
23
PDB code
3rw9
Structure name
crystal structure of human spermidine synthase in complex with decarboxylated s-adenosylhomocysteine
Structure deposition date
2011-05-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
93
Minimum pKa ?
14
% buried
99
Peptide accession
P19623
Residue number A
204
Residue number B
251
Peptide name
Spermidine synthase

Ligandability

Cysteine 204 of Spermidine synthase

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 251 of Spermidine synthase

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 Spermidine synthase between cysteines 204 and 236. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
21
PDB code
3rw9
Structure name
crystal structure of human spermidine synthase in complex with decarboxylated s-adenosylhomocysteine
Structure deposition date
2011-05-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
93
Minimum pKa ?
13
% buried
100
Peptide accession
P19623
Residue number A
204
Residue number B
236
Peptide name
Spermidine synthase

Ligandability

Cysteine 204 of Spermidine synthase

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 236 of Spermidine synthase

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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