ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Nicotinamide N-methyltransferase

Intramolecular
Cysteine 141 and cysteine 165
Cysteine 75 and cysteine 115
Cysteine 170 and cysteine 177
Cysteine 165 and cysteine 170
Cysteine 50 and cysteine 75
A redox-regulated disulphide may form within Nicotinamide N-methyltransferase between cysteines 141 and 165. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
7nbm
Structure name
co-crystal structure of human nicotinamide n-methyltransferase (nnmt) with the bisubstrate-like inhibitor (33)
Structure deposition date
2021-01-27
Thiol separation (Å)
6
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
100
Peptide accession
P40261
Residue number A
141
Residue number B
165
Peptide name
Nicotinamide N-methyltransferase

Ligandability

Cysteine 141 of Nicotinamide 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 165 of Nicotinamide 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 Nicotinamide 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 ?
41
PDB code
7egu
Structure name
structure of human nnmt in complex with macrocyclic peptide x
Structure deposition date
2021-03-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
60
Peptide accession
P40261
Residue number A
75
Residue number B
115
Peptide name
Nicotinamide N-methyltransferase

Ligandability

Cysteine 75 of Nicotinamide 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 Nicotinamide 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 Nicotinamide N-methyltransferase between cysteines 170 and 177. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
7et7
Structure name
co-crystal structure of human nicotinamide n-methyltransferase (nnmt) with tricyclic small molecule inhibitor jbsnf-000028
Structure deposition date
2021-05-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
58
Peptide accession
P40261
Residue number A
170
Residue number B
177
Peptide name
Nicotinamide N-methyltransferase

Ligandability

Cysteine 170 of Nicotinamide 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 177 of Nicotinamide 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 Nicotinamide N-methyltransferase between cysteines 165 and 170. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7egu
Structure name
structure of human nnmt in complex with macrocyclic peptide x
Structure deposition date
2021-03-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
12
% buried
88
Peptide accession
P40261
Residue number A
165
Residue number B
170
Peptide name
Nicotinamide N-methyltransferase

Ligandability

Cysteine 165 of Nicotinamide 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 Nicotinamide 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 Nicotinamide N-methyltransferase between cysteines 50 and 75. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
2iip
Structure name
human nicotinamide n-methyltransferase
Structure deposition date
2006-09-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
75
Peptide accession
P40261
Residue number A
50
Residue number B
75
Peptide name
Nicotinamide N-methyltransferase

Ligandability

Cysteine 50 of Nicotinamide 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 75 of Nicotinamide 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.

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