ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase

Intramolecular
Cysteine 181 and cysteine 253
Cysteine 181 and cysteine 228
Cysteine 253 and cysteine 255
Cysteine 86 and cysteine 95
A redox-regulated disulphide may form within Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase between cysteines 181 and 253 (1181 and 1253 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
2o4u
Structure name
crystal structure of mammalian dimeric dihydrodiol dehydrogenase
Structure deposition date
2006-12-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
83
Minimum pKa ?
13
% buried
nan
Peptide accession
Q9TQS6
Residue number A
181
Residue number B
253
Peptide name
Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase

Ligandability

Cysteine 181 of Trans-1,2-dihydrobenzene-1,2-diol 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 253 of Trans-1,2-dihydrobenzene-1,2-diol 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 Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase between cysteines 181 and 228 (1181 and 1228 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
2o48
Structure name
crystal structure of mammalian dimeric dihydrodiol dehydrogenase
Structure deposition date
2006-12-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
88
Minimum pKa ?
13
% buried
100
Peptide accession
Q9TQS6
Residue number A
181
Residue number B
228
Peptide name
Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase

Ligandability

Cysteine 181 of Trans-1,2-dihydrobenzene-1,2-diol 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 228 of Trans-1,2-dihydrobenzene-1,2-diol 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 Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase between cysteines 253 and 255 (1253 and 1255 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
2o48
Structure name
crystal structure of mammalian dimeric dihydrodiol dehydrogenase
Structure deposition date
2006-12-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
13
% buried
nan
Peptide accession
Q9TQS6
Residue number A
253
Residue number B
255
Peptide name
Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase

Ligandability

Cysteine 253 of Trans-1,2-dihydrobenzene-1,2-diol 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 255 of Trans-1,2-dihydrobenzene-1,2-diol 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 Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase between cysteines 86 and 95 (1086 and 1095 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
3ohs
Structure name
crystal structure of mammalian dimeric dihydrodiol dehydrogenase in complex with dihydroxyacetone
Structure deposition date
2010-08-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
91
Minimum pKa ?
12
% buried
98
Peptide accession
Q9TQS6
Residue number A
86
Residue number B
95
Peptide name
Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase

Ligandability

Cysteine 86 of Trans-1,2-dihydrobenzene-1,2-diol 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 95 of Trans-1,2-dihydrobenzene-1,2-diol 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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