ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

tRNA N(3)-methylcytidine methyltransferase METTL6

Intramolecular
Cysteine 109 and cysteine 135
Cysteine 88 and cysteine 130
Cysteine 88 and cysteine 109
Cysteine 88 and cysteine 93
A redox-regulated disulphide may form within tRNA N(3)-methylcytidine methyltransferase METTL6 between cysteines 109 and 135.

Details

Redox score ?
66
PDB code
7f1e
Structure name
structure of mettl6 bound with sam
Structure deposition date
2021-06-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
9
% buried
86
Peptide accession
Q8TCB7
Residue number A
109
Residue number B
135
Peptide name
tRNA N(3)-methylcytidine methyltransferase METTL6

Ligandability

Cysteine 109 of tRNA N(3)-methylcytidine methyltransferase METTL6

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 135 of tRNA N(3)-methylcytidine methyltransferase METTL6

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 tRNA N(3)-methylcytidine methyltransferase METTL6 between cysteines 88 and 130. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
7ezg
Structure name
the structure of the human mettl6 enzyme in complex with sah
Structure deposition date
2021-06-01
Thiol separation (Å)
7
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
89
Peptide accession
Q8TCB7
Residue number A
88
Residue number B
130
Peptide name
tRNA N(3)-methylcytidine methyltransferase METTL6

Ligandability

Cysteine 88 of tRNA N(3)-methylcytidine methyltransferase METTL6

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 130 of tRNA N(3)-methylcytidine methyltransferase METTL6

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 tRNA N(3)-methylcytidine methyltransferase METTL6 between cysteines 88 and 109. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
7f1e
Structure name
structure of mettl6 bound with sam
Structure deposition date
2021-06-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
84
Minimum pKa ?
15
% buried
100
Peptide accession
Q8TCB7
Residue number A
88
Residue number B
109
Peptide name
tRNA N(3)-methylcytidine methyltransferase METTL6

Ligandability

Cysteine 88 of tRNA N(3)-methylcytidine methyltransferase METTL6

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 109 of tRNA N(3)-methylcytidine methyltransferase METTL6

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 tRNA N(3)-methylcytidine methyltransferase METTL6 between cysteines 88 and 93. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
25
PDB code
7f1e
Structure name
structure of mettl6 bound with sam
Structure deposition date
2021-06-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
13
% buried
92
Peptide accession
Q8TCB7
Residue number A
88
Residue number B
93
Peptide name
tRNA N(3)-methylcytidine methyltransferase METTL6

Ligandability

Cysteine 88 of tRNA N(3)-methylcytidine methyltransferase METTL6

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 93 of tRNA N(3)-methylcytidine methyltransferase METTL6

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: