ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

RNA 5'-monophosphate methyltransferase

Intermolecular
Cysteine 249 and cysteine 249
Cysteine 248 and cysteine 249
Cysteine 248 and cysteine 248
Intramolecular
Cysteine 75 and cysteine 108
Cysteine 108 and cysteine 123
Cysteine 75 and cysteine 109
Cysteine 108 and cysteine 109
Cysteine 75 and cysteine 123
Cysteine 163 and cysteine 190
Cysteine 109 and cysteine 190
Cysteine 109 and cysteine 163
A redox-regulated disulphide may form between two units of RNA 5'-monophosphate methyltransferase at cysteines 249 and 249.

Details

Redox score ?
64
PDB code
6l8u
Structure name
crystal structure of human bcdin3d in complex with sah
Structure deposition date
2019-11-07
Thiol separation (Å)
5
Half-sphere exposure sum ?
80
Minimum pKa ?
8
% buried
100
Peptide A name
RNA 5'-monophosphate methyltransferase
Peptide B name
RNA 5'-monophosphate methyltransferase
Peptide A accession
Q7Z5W3
Peptide B accession
Q7Z5W3
Peptide A residue number
249
Peptide B residue number
249

Ligandability

A redox-regulated disulphide may form between two units of RNA 5'-monophosphate methyltransferase at cysteines 248 and 249. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
6l8u
Structure name
crystal structure of human bcdin3d in complex with sah
Structure deposition date
2019-11-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
77
Minimum pKa ?
13
% buried
100
Peptide A name
RNA 5'-monophosphate methyltransferase
Peptide B name
RNA 5'-monophosphate methyltransferase
Peptide A accession
Q7Z5W3
Peptide B accession
Q7Z5W3
Peptide A residue number
248
Peptide B residue number
249

Ligandability

Cysteine 248 of RNA 5'-monophosphate methyltransferase

Cysteine 249 of RNA 5'-monophosphate methyltransferase

A redox-regulated disulphide may form between two units of RNA 5'-monophosphate methyltransferase at cysteines 248 and 248. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
6l8u
Structure name
crystal structure of human bcdin3d in complex with sah
Structure deposition date
2019-11-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
13
% buried
100
Peptide A name
RNA 5'-monophosphate methyltransferase
Peptide B name
RNA 5'-monophosphate methyltransferase
Peptide A accession
Q7Z5W3
Peptide B accession
Q7Z5W3
Peptide A residue number
248
Peptide B residue number
248

Ligandability

A redox-regulated disulphide may form within RNA 5'-monophosphate methyltransferase between cysteines 75 and 108. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
6l8u
Structure name
crystal structure of human bcdin3d in complex with sah
Structure deposition date
2019-11-07
Thiol separation (Å)
5
Half-sphere exposure sum ?
97
Minimum pKa ?
9
% buried
100
Peptide accession
Q7Z5W3
Residue number A
75
Residue number B
108
Peptide name
RNA 5'-monophosphate methyltransferase

Ligandability

Cysteine 75 of RNA 5'-monophosphate methyltransferase

Cysteine 108 of RNA 5'-monophosphate methyltransferase

A redox-regulated disulphide may form within RNA 5'-monophosphate methyltransferase between cysteines 108 and 123. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
6l8u
Structure name
crystal structure of human bcdin3d in complex with sah
Structure deposition date
2019-11-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
69
Peptide accession
Q7Z5W3
Residue number A
108
Residue number B
123
Peptide name
RNA 5'-monophosphate methyltransferase

Ligandability

Cysteine 108 of RNA 5'-monophosphate methyltransferase

Cysteine 123 of RNA 5'-monophosphate methyltransferase

A redox-regulated disulphide may form within RNA 5'-monophosphate methyltransferase between cysteines 75 and 109. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
6l8u
Structure name
crystal structure of human bcdin3d in complex with sah
Structure deposition date
2019-11-07
Thiol separation (Å)
6
Half-sphere exposure sum ?
91
Minimum pKa ?
13
% buried
100
Peptide accession
Q7Z5W3
Residue number A
75
Residue number B
109
Peptide name
RNA 5'-monophosphate methyltransferase

Ligandability

Cysteine 75 of RNA 5'-monophosphate methyltransferase

Cysteine 109 of RNA 5'-monophosphate methyltransferase

A redox-regulated disulphide may form within RNA 5'-monophosphate methyltransferase between cysteines 108 and 109. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
6l8u
Structure name
crystal structure of human bcdin3d in complex with sah
Structure deposition date
2019-11-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
84
Minimum pKa ?
10
% buried
100
Peptide accession
Q7Z5W3
Residue number A
108
Residue number B
109
Peptide name
RNA 5'-monophosphate methyltransferase

Ligandability

Cysteine 108 of RNA 5'-monophosphate methyltransferase

Cysteine 109 of RNA 5'-monophosphate methyltransferase

A redox-regulated disulphide may form within RNA 5'-monophosphate methyltransferase between cysteines 75 and 123. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
6l8u
Structure name
crystal structure of human bcdin3d in complex with sah
Structure deposition date
2019-11-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
10
% buried
66
Peptide accession
Q7Z5W3
Residue number A
75
Residue number B
123
Peptide name
RNA 5'-monophosphate methyltransferase

Ligandability

Cysteine 75 of RNA 5'-monophosphate methyltransferase

Cysteine 123 of RNA 5'-monophosphate methyltransferase

A redox-regulated disulphide may form within RNA 5'-monophosphate methyltransferase between cysteines 163 and 190. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
6l8u
Structure name
crystal structure of human bcdin3d in complex with sah
Structure deposition date
2019-11-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
100
Peptide accession
Q7Z5W3
Residue number A
163
Residue number B
190
Peptide name
RNA 5'-monophosphate methyltransferase

Ligandability

Cysteine 163 of RNA 5'-monophosphate methyltransferase

Cysteine 190 of RNA 5'-monophosphate methyltransferase

A redox-regulated disulphide may form within RNA 5'-monophosphate methyltransferase between cysteines 109 and 190. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
6l8u
Structure name
crystal structure of human bcdin3d in complex with sah
Structure deposition date
2019-11-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
13
% buried
100
Peptide accession
Q7Z5W3
Residue number A
109
Residue number B
190
Peptide name
RNA 5'-monophosphate methyltransferase

Ligandability

Cysteine 109 of RNA 5'-monophosphate methyltransferase

Cysteine 190 of RNA 5'-monophosphate methyltransferase

A redox-regulated disulphide may form within RNA 5'-monophosphate methyltransferase between cysteines 109 and 163. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
22
PDB code
6l8u
Structure name
crystal structure of human bcdin3d in complex with sah
Structure deposition date
2019-11-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
100
Peptide accession
Q7Z5W3
Residue number A
109
Residue number B
163
Peptide name
RNA 5'-monophosphate methyltransferase

Ligandability

Cysteine 109 of RNA 5'-monophosphate methyltransferase

Cysteine 163 of RNA 5'-monophosphate methyltransferase

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