ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Calmodulin-lysine N-methyltransferase

Intramolecular
Cysteine 230 and cysteine 233
Cysteine 151 and cysteine 208
Cysteine 151 and cysteine 159
Cysteine 159 and cysteine 233
Cysteine 151 and cysteine 230
Cysteine 159 and cysteine 208
A redox-regulated disulphide may form within Calmodulin-lysine N-methyltransferase between cysteines 230 and 233.

Details

Redox score ?
63
PDB code
4pwy
Structure name
crystal structure of a calmodulin-lysine n-methyltransferase fragment
Structure deposition date
2014-03-21
Thiol separation (Å)
5
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q7Z624
Residue number A
230
Residue number B
233
Peptide name
Calmodulin-lysine N-methyltransferase

Ligandability

Cysteine 230 of Calmodulin-lysine 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 233 of Calmodulin-lysine 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 Calmodulin-lysine N-methyltransferase between cysteines 151 and 208. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
4pwy
Structure name
crystal structure of a calmodulin-lysine n-methyltransferase fragment
Structure deposition date
2014-03-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q7Z624
Residue number A
151
Residue number B
208
Peptide name
Calmodulin-lysine N-methyltransferase

Ligandability

Cysteine 151 of Calmodulin-lysine 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 208 of Calmodulin-lysine 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 Calmodulin-lysine N-methyltransferase between cysteines 151 and 159. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
4pwy
Structure name
crystal structure of a calmodulin-lysine n-methyltransferase fragment
Structure deposition date
2014-03-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
99
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q7Z624
Residue number A
151
Residue number B
159
Peptide name
Calmodulin-lysine N-methyltransferase

Ligandability

Cysteine 151 of Calmodulin-lysine 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 159 of Calmodulin-lysine 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 Calmodulin-lysine N-methyltransferase between cysteines 159 and 233. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
4pwy
Structure name
crystal structure of a calmodulin-lysine n-methyltransferase fragment
Structure deposition date
2014-03-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q7Z624
Residue number A
159
Residue number B
233
Peptide name
Calmodulin-lysine N-methyltransferase

Ligandability

Cysteine 159 of Calmodulin-lysine 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 233 of Calmodulin-lysine 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 Calmodulin-lysine N-methyltransferase between cysteines 151 and 230. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
4pwy
Structure name
crystal structure of a calmodulin-lysine n-methyltransferase fragment
Structure deposition date
2014-03-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
93
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q7Z624
Residue number A
151
Residue number B
230
Peptide name
Calmodulin-lysine N-methyltransferase

Ligandability

Cysteine 151 of Calmodulin-lysine 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 230 of Calmodulin-lysine 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 Calmodulin-lysine N-methyltransferase between cysteines 159 and 208. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
4pwy
Structure name
crystal structure of a calmodulin-lysine n-methyltransferase fragment
Structure deposition date
2014-03-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q7Z624
Residue number A
159
Residue number B
208
Peptide name
Calmodulin-lysine N-methyltransferase

Ligandability

Cysteine 159 of Calmodulin-lysine 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 208 of Calmodulin-lysine 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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