a tool for identifying drug-targetable redox-active disulphides

Dehydrogenase/reductase SDR family member 6

Intermolecular

Cysteine 145 and cysteine 172

Intramolecular

Cysteine 174 and cysteine 176

Cysteine 93 and cysteine 145

Cysteine 172 and cysteine 174

A redox-regulated disulphide may form between two units of Dehydrogenase/reductase SDR family member 6 at cysteines 145 and 172. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

25

PDB code

Structure name

crystal structure of human dhrs6

Structure deposition date

2005-07-26

Thiol separation (Å)

10

Half-sphere exposure sum ?

95

Minimum pK_a ?

13

% buried

100

Peptide A name

Dehydrogenase/reductase SDR family member 6

Peptide B name

Dehydrogenase/reductase SDR family member 6

Peptide A accession

Peptide B accession

Peptide A residue number

145

Peptide B residue number

172

Ligandability

Cysteine 145 of Dehydrogenase/reductase SDR family member 6

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 172 of Dehydrogenase/reductase SDR family member 6

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 Dehydrogenase/reductase SDR family member 6 between cysteines 174 and 176.

Details

Redox score ?

64

PDB code

Structure name

crystal structure of human dhrs6

Structure deposition date

2005-07-26

Thiol separation (Å)

4

Half-sphere exposure sum ?

84

Minimum pK_a ?

8

% buried

100

Peptide accession

Residue number A

174

Residue number B

176

Peptide name

Dehydrogenase/reductase SDR family member 6

Ligandability

Cysteine 174 of Dehydrogenase/reductase SDR family member 6

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 176 of Dehydrogenase/reductase SDR family member 6

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 Dehydrogenase/reductase SDR family member 6 between cysteines 93 and 145. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

59

PDB code

Structure name

crystal structure of human dhrs6

Structure deposition date

2005-07-26

Thiol separation (Å)

6

Half-sphere exposure sum ?

75

Minimum pK_a ?

9

% buried

86

Peptide accession

Residue number A

93

Residue number B

145

Peptide name

Dehydrogenase/reductase SDR family member 6

Ligandability

Cysteine 93 of Dehydrogenase/reductase SDR family member 6

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 145 of Dehydrogenase/reductase SDR family member 6

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 Dehydrogenase/reductase SDR family member 6 between cysteines 172 and 174. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

37

PDB code

Structure name

crystal structure of human dhrs6

Structure deposition date

2005-07-26

Thiol separation (Å)

7

Half-sphere exposure sum ?

94

Minimum pK_a ?

13

% buried

100

Peptide accession

Residue number A

172

Residue number B

174

Peptide name

Dehydrogenase/reductase SDR family member 6

Ligandability

Cysteine 172 of Dehydrogenase/reductase SDR family member 6

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 174 of Dehydrogenase/reductase SDR family member 6

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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