ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Dehydrogenase/reductase SDR family member 11

Intramolecular
Cysteine 41 and cysteine 69
Cysteine 69 and cysteine 128
Cysteine 94 and cysteine 128
Cysteine 41 and cysteine 128
Cysteine 41 and cysteine 94
A redox-regulated disulphide may form within Dehydrogenase/reductase SDR family member 11 between cysteines 41 and 69.

Details

Redox score ?
65
PDB code
1xg5
Structure name
structure of human putative dehydrogenase mgc4172 in complex with nadp
Structure deposition date
2004-09-16
Thiol separation (Å)
5
Half-sphere exposure sum ?
77
Minimum pKa ?
8
% buried
84
Peptide accession
Q6UWP2
Residue number A
41
Residue number B
69
Peptide name
Dehydrogenase/reductase SDR family member 11

Ligandability

Cysteine 41 of Dehydrogenase/reductase SDR family member 11

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 Dehydrogenase/reductase SDR family member 11

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 11 between cysteines 69 and 128. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
1xg5
Structure name
structure of human putative dehydrogenase mgc4172 in complex with nadp
Structure deposition date
2004-09-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
85
Minimum pKa ?
9
% buried
85
Peptide accession
Q6UWP2
Residue number A
69
Residue number B
128
Peptide name
Dehydrogenase/reductase SDR family member 11

Ligandability

Cysteine 69 of Dehydrogenase/reductase SDR family member 11

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 128 of Dehydrogenase/reductase SDR family member 11

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 11 between cysteines 94 and 128. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
1xg5
Structure name
structure of human putative dehydrogenase mgc4172 in complex with nadp
Structure deposition date
2004-09-16
Thiol separation (Å)
5
Half-sphere exposure sum ?
96
Minimum pKa ?
12
% buried
100
Peptide accession
Q6UWP2
Residue number A
94
Residue number B
128
Peptide name
Dehydrogenase/reductase SDR family member 11

Ligandability

Cysteine 94 of Dehydrogenase/reductase SDR family member 11

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 128 of Dehydrogenase/reductase SDR family member 11

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 11 between cysteines 41 and 128. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
1xg5
Structure name
structure of human putative dehydrogenase mgc4172 in complex with nadp
Structure deposition date
2004-09-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
93
Minimum pKa ?
14
% buried
100
Peptide accession
Q6UWP2
Residue number A
41
Residue number B
128
Peptide name
Dehydrogenase/reductase SDR family member 11

Ligandability

Cysteine 41 of Dehydrogenase/reductase SDR family member 11

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 128 of Dehydrogenase/reductase SDR family member 11

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 11 between cysteines 41 and 94. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
1xg5
Structure name
structure of human putative dehydrogenase mgc4172 in complex with nadp
Structure deposition date
2004-09-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
90
Minimum pKa ?
12
% buried
100
Peptide accession
Q6UWP2
Residue number A
41
Residue number B
94
Peptide name
Dehydrogenase/reductase SDR family member 11

Ligandability

Cysteine 41 of Dehydrogenase/reductase SDR family member 11

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 94 of Dehydrogenase/reductase SDR family member 11

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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