ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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N-terminal Xaa-Pro-Lys N-methyltransferase 1

Intramolecular
Cysteine 68 and cysteine 153 L
Cysteine 116 and cysteine 117
Cysteine 68 and cysteine 117 L
A redox-regulated disulphide may form within N-terminal Xaa-Pro-Lys N-methyltransferase 1 between cysteines 68 and 153.

Details

Redox score ?
60
PDB code
6kdq
Structure name
crystal structure of human nrmt1 in complex with alpha-n- monomethylated human cenp-a peptide
Structure deposition date
2019-07-02
Thiol separation (Å)
5
Half-sphere exposure sum ?
88
Minimum pKa ?
9
% buried
100
Peptide accession
Q9BV86
Residue number A
68
Residue number B
153
Peptide name
N-terminal Xaa-Pro-Lys N-methyltransferase 1

Ligandability

Cysteine 68 of N-terminal Xaa-Pro-Lys N-methyltransferase 1

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 153 of N-terminal Xaa-Pro-Lys N-methyltransferase 1

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 N-terminal Xaa-Pro-Lys N-methyltransferase 1 between cysteines 116 and 117. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
6dtn
Structure name
the structure of ntmt1 in complex with compound dc100-1
Structure deposition date
2018-06-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
47
Minimum pKa ?
10
% buried
31
Peptide accession
Q9BV86
Residue number A
116
Residue number B
117
Peptide name
N-terminal Xaa-Pro-Lys N-methyltransferase 1

Ligandability

Cysteine 116 of N-terminal Xaa-Pro-Lys N-methyltransferase 1

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 117 of N-terminal Xaa-Pro-Lys N-methyltransferase 1

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 N-terminal Xaa-Pro-Lys N-methyltransferase 1 between cysteines 68 and 117. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
25
PDB code
7u1m
Structure name
crystal structure of ntmt1 in complex with compound yd206
Structure deposition date
2022-02-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
14
% buried
87
Peptide accession
Q9BV86
Residue number A
68
Residue number B
117
Peptide name
N-terminal Xaa-Pro-Lys N-methyltransferase 1

Ligandability

Cysteine 68 of N-terminal Xaa-Pro-Lys N-methyltransferase 1

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 117 of N-terminal Xaa-Pro-Lys N-methyltransferase 1

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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