ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Methyltransferase like 27

Intramolecular
Cysteine 57 and cysteine 165
Cysteine 57 and cysteine 196
Cysteine 165 and cysteine 196
Cysteine 76 and cysteine 165
A redox-regulated disulphide may form within Methyltransferase like 27 between cysteines 57 and 165 (59 and 167 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
7qcb
Structure name
williams-beuren syndrome related methyltransferase wbscr27 in complex with sah
Structure deposition date
2021-11-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
81
Minimum pKa ?
10
% buried
66
Peptide accession
Q8BGM4
Residue number A
57
Residue number B
165
Peptide name
Methyltransferase like 27

Ligandability

Cysteine 57 of Methyltransferase like 27

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 165 of Methyltransferase like 27

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 Methyltransferase like 27 between cysteines 57 and 196 (59 and 198 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
7qcb
Structure name
williams-beuren syndrome related methyltransferase wbscr27 in complex with sah
Structure deposition date
2021-11-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
42
Peptide accession
Q8BGM4
Residue number A
57
Residue number B
196
Peptide name
Methyltransferase like 27

Ligandability

Cysteine 57 of Methyltransferase like 27

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 196 of Methyltransferase like 27

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 Methyltransferase like 27 between cysteines 165 and 196 (167 and 198 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
7qcc
Structure name
williams-beuren syndrome related methyltransferase wbscr27 in apo-form
Structure deposition date
2021-11-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
10
% buried
76
Peptide accession
Q8BGM4
Residue number A
165
Residue number B
196
Peptide name
Methyltransferase like 27

Ligandability

Cysteine 165 of Methyltransferase like 27

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 196 of Methyltransferase like 27

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 Methyltransferase like 27 between cysteines 76 and 165 (78 and 167 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
25
PDB code
7qcc
Structure name
williams-beuren syndrome related methyltransferase wbscr27 in apo-form
Structure deposition date
2021-11-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
86
Peptide accession
Q8BGM4
Residue number A
76
Residue number B
165
Peptide name
Methyltransferase like 27

Ligandability

Cysteine 76 of Methyltransferase like 27

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 165 of Methyltransferase like 27

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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