ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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NNMT protein

Intramolecular
Cysteine 141 and cysteine 165
Cysteine 165 and cysteine 170
Cysteine 170 and cysteine 177
Cysteine 75 and cysteine 115
Cysteine 50 and cysteine 75
A redox-regulated disulphide may form within NNMT protein 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 ?
49
PDB code
7sok
Structure name
structure of nicotinamide n-methyltransferase (nnmt) in complex with inhibitor ii329
Structure deposition date
2021-10-31
Thiol separation (Å)
6
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
100
Peptide accession
Q6FH49
Residue number A
141
Residue number B
165
Peptide name
NNMT protein

Ligandability

Cysteine 141 of NNMT protein

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 NNMT protein

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 NNMT protein 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 ?
42
PDB code
7rkl
Structure name
structure of nicotinamide n-methyltransferase (nnmt) in complex with ii399 (p1 space group)
Structure deposition date
2021-07-22
Thiol separation (Å)
7
Half-sphere exposure sum ?
71
Minimum pKa ?
13
% buried
100
Peptide accession
Q6FH49
Residue number A
165
Residue number B
170
Peptide name
NNMT protein

Ligandability

Cysteine 165 of NNMT protein

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 NNMT protein

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 NNMT protein 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
7sok
Structure name
structure of nicotinamide n-methyltransferase (nnmt) in complex with inhibitor ii329
Structure deposition date
2021-10-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
60
Peptide accession
Q6FH49
Residue number A
170
Residue number B
177
Peptide name
NNMT protein

Ligandability

Cysteine 170 of NNMT protein

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 NNMT protein

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 NNMT protein 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
6pve
Structure name
structure of nicotinamide n-methyltransferase (nnmt) in complex with inhibitor ll319
Structure deposition date
2019-07-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
58
Peptide accession
Q6FH49
Residue number A
75
Residue number B
115
Peptide name
NNMT protein

Ligandability

Cysteine 75 of NNMT protein

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 NNMT protein

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 NNMT protein 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
6pvs
Structure name
structure of nicotinamide n-methyltransferase (nnmt) in complex with inhibitor ll320
Structure deposition date
2019-07-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
12
% buried
74
Peptide accession
Q6FH49
Residue number A
50
Residue number B
75
Peptide name
NNMT protein

Ligandability

Cysteine 50 of NNMT protein

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 NNMT protein

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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