ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Serine dehydratase-like

Intramolecular
Cysteine 276 and cysteine 309
Cysteine 241 and cysteine 245
Cysteine 56 and cysteine 64
Cysteine 56 and cysteine 69
Cysteine 38 and cysteine 276
A redox-regulated disulphide may form within Serine dehydratase-like between cysteines 276 and 309.

Details

Redox score ?
62
PDB code
2rkb
Structure name
serine dehydratase like-1 from human cancer cells
Structure deposition date
2007-10-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
103
Minimum pKa ?
9
% buried
100
Peptide accession
Q96GA7
Residue number A
276
Residue number B
309
Peptide name
Serine dehydratase-like

Ligandability

Cysteine 276 of Serine dehydratase-like

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 309 of Serine dehydratase-like

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 Serine dehydratase-like between cysteines 241 and 245. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
2rkb
Structure name
serine dehydratase like-1 from human cancer cells
Structure deposition date
2007-10-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
62
Peptide accession
Q96GA7
Residue number A
241
Residue number B
245
Peptide name
Serine dehydratase-like

Ligandability

Cysteine 241 of Serine dehydratase-like

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 245 of Serine dehydratase-like

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 Serine dehydratase-like between cysteines 56 and 64. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
2rkb
Structure name
serine dehydratase like-1 from human cancer cells
Structure deposition date
2007-10-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
76
Minimum pKa ?
10
% buried
69
Peptide accession
Q96GA7
Residue number A
56
Residue number B
64
Peptide name
Serine dehydratase-like

Ligandability

Cysteine 56 of Serine dehydratase-like

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 64 of Serine dehydratase-like

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 Serine dehydratase-like between cysteines 56 and 69. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
2rkb
Structure name
serine dehydratase like-1 from human cancer cells
Structure deposition date
2007-10-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
97
Minimum pKa ?
11
% buried
100
Peptide accession
Q96GA7
Residue number A
56
Residue number B
69
Peptide name
Serine dehydratase-like

Ligandability

Cysteine 56 of Serine dehydratase-like

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 69 of Serine dehydratase-like

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 Serine dehydratase-like between cysteines 38 and 276. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
2rkb
Structure name
serine dehydratase like-1 from human cancer cells
Structure deposition date
2007-10-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
98
Minimum pKa ?
9
% buried
100
Peptide accession
Q96GA7
Residue number A
38
Residue number B
276
Peptide name
Serine dehydratase-like

Ligandability

Cysteine 38 of Serine dehydratase-like

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 276 of Serine dehydratase-like

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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