ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Thiopurine S-methyltransferase

Intermolecular
Cysteine 165 and cysteine 165
Intramolecular
Cysteine 132 and cysteine 133
Cysteine 70 and cysteine 132
Cysteine 65 and cysteine 128
A redox-regulated disulphide may form between two units of Thiopurine S-methyltransferase at cysteines 165 and 165. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
2h11
Structure name
amino-terminal truncated thiopurine s-methyltransferase complexed with s-adenosyl-l-homocysteine
Structure deposition date
2006-05-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
100
Peptide A name
Thiopurine S-methyltransferase
Peptide B name
Thiopurine S-methyltransferase
Peptide A accession
O43213
Peptide B accession
O43213
Peptide A residue number
165
Peptide B residue number
165

Ligandability

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 Thiopurine S-methyltransferase between cysteines 132 and 133. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2bzg
Structure name
crystal structure of thiopurine s-methyltransferase
Structure deposition date
2005-08-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
76
Peptide accession
P51580
Residue number A
132
Residue number B
133
Peptide name
Thiopurine S-methyltransferase

Ligandability

Cysteine 132 of Thiopurine S-methyltransferase

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 133 of Thiopurine S-methyltransferase

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 Thiopurine S-methyltransferase between cysteines 70 and 132. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
2h11
Structure name
amino-terminal truncated thiopurine s-methyltransferase complexed with s-adenosyl-l-homocysteine
Structure deposition date
2006-05-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
90
Peptide accession
O43213
Residue number A
70
Residue number B
132
Peptide name
Thiopurine S-methyltransferase

Ligandability

Cysteine 70 of Thiopurine S-methyltransferase

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 132 of Thiopurine S-methyltransferase

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 Thiopurine S-methyltransferase between cysteines 65 and 128. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
3bgi
Structure name
thiopurine s-methyltransferase
Structure deposition date
2007-11-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
13
% buried
93
Peptide accession
O55060
Residue number A
65
Residue number B
128
Peptide name
Thiopurine S-methyltransferase

Ligandability

Cysteine 65 of Thiopurine S-methyltransferase

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 Thiopurine S-methyltransferase

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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