ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Sorbitol dehydrogenase

Intramolecular
Cysteine 130 and cysteine 350 L
Cysteine 106 and cysteine 301 L
Cysteine 179 and cysteine 250
Cysteine 120 and cysteine 140 L
Cysteine 120 and cysteine 130 L
Cysteine 165 and cysteine 250
A redox-regulated disulphide may form within Sorbitol dehydrogenase between cysteines 130 and 350 (129 and 349 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
1pl6
Structure name
human sdh/nadh/inhibitor complex
Structure deposition date
2003-06-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
85
Minimum pKa ?
12
% buried
100
Peptide accession
Q00796
Residue number A
130
Residue number B
350
Peptide name
Sorbitol dehydrogenase

Ligandability

Cysteine 130 of Sorbitol dehydrogenase

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 350 of Sorbitol dehydrogenase

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 Sorbitol dehydrogenase between cysteines 106 and 301 (105 and 300 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
1pl8
Structure name
human sdh/nad+ complex
Structure deposition date
2003-06-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
32
Peptide accession
Q00796
Residue number A
106
Residue number B
301
Peptide name
Sorbitol dehydrogenase

Ligandability

Cysteine 106 of Sorbitol dehydrogenase

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 301 of Sorbitol dehydrogenase

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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sorbitol dehydrogenase between cysteines 179 and 250 (178 and 249 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
1pl8
Structure name
human sdh/nad+ complex
Structure deposition date
2003-06-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
95
Minimum pKa ?
12
% buried
100
Peptide accession
Q00796
Residue number A
179
Residue number B
250
Peptide name
Sorbitol dehydrogenase

Ligandability

Cysteine 179 of Sorbitol dehydrogenase

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 250 of Sorbitol dehydrogenase

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 Sorbitol dehydrogenase between cysteines 120 and 140 (119 and 139 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
1pl8
Structure name
human sdh/nad+ complex
Structure deposition date
2003-06-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
100
Peptide accession
Q00796
Residue number A
120
Residue number B
140
Peptide name
Sorbitol dehydrogenase

Ligandability

Cysteine 120 of Sorbitol dehydrogenase

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 140 of Sorbitol dehydrogenase

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 Sorbitol dehydrogenase between cysteines 120 and 130 (119 and 129 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
1pl8
Structure name
human sdh/nad+ complex
Structure deposition date
2003-06-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
100
Peptide accession
Q00796
Residue number A
120
Residue number B
130
Peptide name
Sorbitol dehydrogenase

Ligandability

Cysteine 120 of Sorbitol dehydrogenase

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 130 of Sorbitol dehydrogenase

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 Sorbitol dehydrogenase between cysteines 165 and 250 (164 and 249 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
1pl7
Structure name
human sorbitol dehydrogenase (apo)
Structure deposition date
2003-06-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
89
Minimum pKa ?
13
% buried
100
Peptide accession
Q00796
Residue number A
165
Residue number B
250
Peptide name
Sorbitol dehydrogenase

Ligandability

Cysteine 165 of Sorbitol dehydrogenase

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 250 of Sorbitol dehydrogenase

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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