ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Protein N-lysine methyltransferase METTL21D

Intramolecular
Cysteine 145 and cysteine 171
Cysteine 171 and cysteine 172
Cysteine 40 and cysteine 145
A redox-regulated disulphide may form within Protein N-lysine methyltransferase METTL21D between cysteines 145 and 171. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
4lg1
Structure name
human methyltransferase-like protein 21d
Structure deposition date
2013-06-27
Thiol separation (Å)
7
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H867
Residue number A
145
Residue number B
171
Peptide name
Protein N-lysine methyltransferase METTL21D

Ligandability

Cysteine 145 of Protein N-lysine methyltransferase METTL21D

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 171 of Protein N-lysine methyltransferase METTL21D

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 Protein N-lysine methyltransferase METTL21D between cysteines 171 and 172. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
4lg1
Structure name
human methyltransferase-like protein 21d
Structure deposition date
2013-06-27
Thiol separation (Å)
7
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H867
Residue number A
171
Residue number B
172
Peptide name
Protein N-lysine methyltransferase METTL21D

Ligandability

Cysteine 171 of Protein N-lysine methyltransferase METTL21D

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 172 of Protein N-lysine methyltransferase METTL21D

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 Protein N-lysine methyltransferase METTL21D between cysteines 40 and 145. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
4lg1
Structure name
human methyltransferase-like protein 21d
Structure deposition date
2013-06-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H867
Residue number A
40
Residue number B
145
Peptide name
Protein N-lysine methyltransferase METTL21D

Ligandability

Cysteine 40 of Protein N-lysine methyltransferase METTL21D

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 145 of Protein N-lysine methyltransferase METTL21D

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: