ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Acetylserotonin O-methyltransferase

Intramolecular
Cysteine 29 and cysteine 103
Cysteine 197 and cysteine 204
Cysteine 29 and cysteine 67
Cysteine 184 and cysteine 273
A redox-regulated disulphide may form within Acetylserotonin O-methyltransferase between cysteines 29 and 103.

Details

Redox score ?
72
PDB code
4a6d
Structure name
crystal structure of human n-acetylserotonin methyltransferase (asmt) in complex with sam
Structure deposition date
2011-11-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
6
% buried
68
Peptide accession
P46597
Residue number A
29
Residue number B
103
Peptide name
Acetylserotonin O-methyltransferase

Ligandability

Cysteine 29 of Acetylserotonin O-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 103 of Acetylserotonin O-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 Acetylserotonin O-methyltransferase between cysteines 197 and 204. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
4a6e
Structure name
crystal structure of human n-acetylserotonin methyltransferase (asmt) in complex with sam and n-acetylserotonin
Structure deposition date
2011-11-01
Thiol separation (Å)
7
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
57
Peptide accession
P46597
Residue number A
197
Residue number B
204
Peptide name
Acetylserotonin O-methyltransferase

Ligandability

Cysteine 197 of Acetylserotonin O-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 204 of Acetylserotonin O-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 Acetylserotonin O-methyltransferase between cysteines 29 and 67. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
4a6d
Structure name
crystal structure of human n-acetylserotonin methyltransferase (asmt) in complex with sam
Structure deposition date
2011-11-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
74
Peptide accession
P46597
Residue number A
29
Residue number B
67
Peptide name
Acetylserotonin O-methyltransferase

Ligandability

Cysteine 29 of Acetylserotonin O-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 67 of Acetylserotonin O-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 Acetylserotonin O-methyltransferase between cysteines 184 and 273. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
4a6e
Structure name
crystal structure of human n-acetylserotonin methyltransferase (asmt) in complex with sam and n-acetylserotonin
Structure deposition date
2011-11-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
83
Peptide accession
P46597
Residue number A
184
Residue number B
273
Peptide name
Acetylserotonin O-methyltransferase

Ligandability

Cysteine 184 of Acetylserotonin O-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 273 of Acetylserotonin O-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.

If this tool was useful for finding a disulphide, please cite: