ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Thioredoxin-like protein 1

Intramolecular
Cysteine 34 and cysteine 37 L
Cysteine 135 and cysteine 137 L
Cysteine 137 and cysteine 149 L
Cysteine 135 and cysteine 149
A redox-regulated disulphide may form within Thioredoxin-like protein 1 between cysteines 34 and 37.

Details

Redox score ?
88
PDB code
1gh2
Structure name
crystal structure of the catalytic domain of a new human thioredoxin-like protein
Structure deposition date
2000-11-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43396
Residue number A
34
Residue number B
37
Peptide name
Thioredoxin-like protein 1

Ligandability

Cysteine 34 of Thioredoxin-like protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

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 37 of Thioredoxin-like protein 1

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 Thioredoxin-like protein 1 between cysteines 135 and 137 (21 and 23 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
1wwy
Structure name
solution structure of the duf1000 domain of a thioredoxin-like protein 1
Structure deposition date
2005-01-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
45
Peptide accession
O43396
Residue number A
135
Residue number B
137
Peptide name
Thioredoxin-like protein 1

Ligandability

Cysteine 135 of Thioredoxin-like protein 1

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 137 of Thioredoxin-like protein 1

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 Thioredoxin-like protein 1 between cysteines 137 and 149 (23 and 35 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
1wwy
Structure name
solution structure of the duf1000 domain of a thioredoxin-like protein 1
Structure deposition date
2005-01-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
66
Peptide accession
O43396
Residue number A
137
Residue number B
149
Peptide name
Thioredoxin-like protein 1

Ligandability

Cysteine 137 of Thioredoxin-like protein 1

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 149 of Thioredoxin-like protein 1

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 Thioredoxin-like protein 1 between cysteines 135 and 149 (21 and 35 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
1wwy
Structure name
solution structure of the duf1000 domain of a thioredoxin-like protein 1
Structure deposition date
2005-01-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
74
Peptide accession
O43396
Residue number A
135
Residue number B
149
Peptide name
Thioredoxin-like protein 1

Ligandability

Cysteine 135 of Thioredoxin-like protein 1

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 149 of Thioredoxin-like protein 1

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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