ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Methylated-DNA--protein-cysteine methyltransferase

Intramolecular
Cysteine 8 and cysteine 27
Cysteine 148 and cysteine 1045
Cysteine 148 and cysteine 1019
Cysteine 1045 and cysteine 1047
A redox-regulated disulphide may form within Methylated-DNA--protein-cysteine methyltransferase between cysteines 8 and 27 (5 and 24 respectively in this structure).

Details

Redox score ?
82
PDB code
3kzy
Structure name
crystal structure of snap-tag
Structure deposition date
2009-12-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
8
% buried
4
Peptide accession
E5BBQ0
Residue number A
8
Residue number B
27
Peptide name
Methylated-DNA--protein-cysteine methyltransferase

Ligandability

Cysteine 8 of Methylated-DNA--protein-cysteine 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 27 of Methylated-DNA--protein-cysteine 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 Methylated-DNA--protein-cysteine methyltransferase between cysteines 148 and 1045 (1018 and 1045 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
8dd7
Structure name
the cryo-em structure of drosophila cryptochrome in complex with timeless
Structure deposition date
2022-06-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
12
% buried
93
Peptide accession
E5BBQ0
Residue number A
148
Residue number B
1045
Peptide name
Methylated-DNA--protein-cysteine methyltransferase

Ligandability

Cysteine 148 of Methylated-DNA--protein-cysteine 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 1045 of Methylated-DNA--protein-cysteine 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 1045 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Methylated-DNA--protein-cysteine methyltransferase between cysteines 148 and 1019 (1018 and 1019 respectively in this structure).

Details

Redox score ?
nan
PDB code
8dd7
Structure name
the cryo-em structure of drosophila cryptochrome in complex with timeless
Structure deposition date
2022-06-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
84
Minimum pKa ?
11
% buried
86
Peptide accession
E5BBQ0
Residue number A
148
Residue number B
1019
Peptide name
Methylated-DNA--protein-cysteine methyltransferase

Ligandability

Cysteine 148 of Methylated-DNA--protein-cysteine 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 1019 of Methylated-DNA--protein-cysteine 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 1019 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Methylated-DNA--protein-cysteine methyltransferase between cysteines 1045 and 1047.

Details

Redox score ?
nan
PDB code
8dd7
Structure name
the cryo-em structure of drosophila cryptochrome in complex with timeless
Structure deposition date
2022-06-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
52
Minimum pKa ?
10
% buried
65
Peptide accession
E5BBQ0
Residue number A
1045
Residue number B
1047
Peptide name
Methylated-DNA--protein-cysteine methyltransferase

Ligandability

Cysteine 1045 of Methylated-DNA--protein-cysteine 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 1047 of Methylated-DNA--protein-cysteine 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 1045 in protein A could not be asigned to a Uniprot residue.
Cysteine 1047 in protein B could not be asigned to a Uniprot residue.
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