ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Indolethylamine N-methyltransferase

Intramolecular
Cysteine 168 and cysteine 213
Cysteine 170 and cysteine 171
Cysteine 75 and cysteine 115
Cysteine 168 and cysteine 170
Cysteine 44 and cysteine 253
Cysteine 44 and cysteine 213
Cysteine 253 and cysteine 213
A redox-regulated disulphide may form within Indolethylamine N-methyltransferase between cysteines 168 and 213.

Details

Redox score ?
66
PDB code
2a14
Structure name
crystal structure of human indolethylamine n- methyltransferase with sah
Structure deposition date
2005-06-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
76
Minimum pKa ?
9
% buried
96
Peptide accession
O95050
Residue number A
168
Residue number B
213
Peptide name
Indolethylamine N-methyltransferase

Ligandability

Cysteine 168 of Indolethylamine N-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 213 of Indolethylamine N-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 Indolethylamine N-methyltransferase between cysteines 170 and 171. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
2a14
Structure name
crystal structure of human indolethylamine n- methyltransferase with sah
Structure deposition date
2005-06-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
61
Minimum pKa ?
9
% buried
42
Peptide accession
O95050
Residue number A
170
Residue number B
171
Peptide name
Indolethylamine N-methyltransferase

Ligandability

Cysteine 170 of Indolethylamine N-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 171 of Indolethylamine N-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 Indolethylamine N-methyltransferase between cysteines 75 and 115. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
2a14
Structure name
crystal structure of human indolethylamine n- methyltransferase with sah
Structure deposition date
2005-06-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
62
Peptide accession
O95050
Residue number A
75
Residue number B
115
Peptide name
Indolethylamine N-methyltransferase

Ligandability

Cysteine 75 of Indolethylamine N-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 115 of Indolethylamine N-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 Indolethylamine N-methyltransferase between cysteines 168 and 170. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
2a14
Structure name
crystal structure of human indolethylamine n- methyltransferase with sah
Structure deposition date
2005-06-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
9
% buried
92
Peptide accession
O95050
Residue number A
168
Residue number B
170
Peptide name
Indolethylamine N-methyltransferase

Ligandability

Cysteine 168 of Indolethylamine N-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 170 of Indolethylamine N-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 Indolethylamine N-methyltransferase between cysteines 44 and 253. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
2a14
Structure name
crystal structure of human indolethylamine n- methyltransferase with sah
Structure deposition date
2005-06-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
12
% buried
66
Peptide accession
O95050
Residue number A
44
Residue number B
253
Peptide name
Indolethylamine N-methyltransferase

Ligandability

Cysteine 44 of Indolethylamine N-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 253 of Indolethylamine N-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 Indolethylamine N-methyltransferase between cysteines 44 and 213 (44 and 254 respectively in this structure).

Details

Redox score ?
nan
PDB code
2a14
Structure name
crystal structure of human indolethylamine n- methyltransferase with sah
Structure deposition date
2005-06-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
8
% buried
85
Peptide accession
O95050
Residue number A
44
Residue number B
213
Peptide name
Indolethylamine N-methyltransferase

Ligandability

Cysteine 44 of Indolethylamine N-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 213 of Indolethylamine N-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.

Uncertain whether structure cysteine 254 has been assigned to correct residue.
A redox-regulated disulphide may form within Indolethylamine N-methyltransferase between cysteines 253 and 213 (253 and 254 respectively in this structure).

Details

Redox score ?
nan
PDB code
2a14
Structure name
crystal structure of human indolethylamine n- methyltransferase with sah
Structure deposition date
2005-06-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
8
% buried
82
Peptide accession
O95050
Residue number A
253
Residue number B
213
Peptide name
Indolethylamine N-methyltransferase

Ligandability

Cysteine 253 of Indolethylamine N-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 213 of Indolethylamine N-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.

Uncertain whether structure cysteine 254 has been assigned to correct residue.
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