ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Methylosome protein 50

Intermolecular
Cysteine 22 of Protein arginine N-methyltransferase 5 and cysteine 53 L
Intramolecular
Cysteine 26 and cysteine 53
Cysteine 172 and cysteine 186
Cysteine 208 and cysteine 247
Cysteine 186 and cysteine 208
Cysteine 186 and cysteine 257
A redox-regulated disulphide may form between cysteine 22 of Protein arginine N-methyltransferase 5 and cysteine 53 of Methylosome protein 50. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
5fa5
Structure name
crystal structure of prmt5:mep50 in complex with mta and h4 peptide
Structure deposition date
2015-12-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
69
Peptide A name
Protein arginine N-methyltransferase 5
Peptide B name
Methylosome protein 50
Peptide A accession
O14744
Peptide B accession
Q9BQA1
Peptide A residue number
22
Peptide B residue number
53

Ligandability

Cysteine 22 of Protein arginine N-methyltransferase 5

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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 53 of Methylosome protein 50

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 Methylosome protein 50 between cysteines 26 and 53. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
60
PDB code
7mxn
Structure name
prmt5(m420t mutant):mep50 complexed with inhibitor pf-06939999
Structure deposition date
2021-05-19
Thiol separation (Å)
6
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
nan
Peptide accession
Q9BQA1
Residue number A
26
Residue number B
53
Peptide name
Methylosome protein 50

Ligandability

Cysteine 26 of Methylosome protein 50

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 53 of Methylosome protein 50

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 Methylosome protein 50 between cysteines 172 and 186. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
8ctb
Structure name
human prmt5:mep50 structure with fragment 3 and mta bound
Structure deposition date
2022-05-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
95
Minimum pKa ?
8
% buried
100
Peptide accession
Q9BQA1
Residue number A
172
Residue number B
186
Peptide name
Methylosome protein 50

Ligandability

Cysteine 172 of Methylosome protein 50

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 186 of Methylosome protein 50

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 Methylosome protein 50 between cysteines 208 and 247. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
7mxn
Structure name
prmt5(m420t mutant):mep50 complexed with inhibitor pf-06939999
Structure deposition date
2021-05-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
4
Peptide accession
Q9BQA1
Residue number A
208
Residue number B
247
Peptide name
Methylosome protein 50

Ligandability

Cysteine 208 of Methylosome protein 50

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 247 of Methylosome protein 50

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 Methylosome protein 50 between cysteines 186 and 208. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
4x60
Structure name
crystal structure of prmt5:mep50 with epz015666 and sinefungin
Structure deposition date
2014-12-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
10
% buried
78
Peptide accession
Q9BQA1
Residue number A
186
Residue number B
208
Peptide name
Methylosome protein 50

Ligandability

Cysteine 186 of Methylosome protein 50

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 Methylosome protein 50

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 Methylosome protein 50 between cysteines 186 and 257. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
20
PDB code
7kic
Structure name
prmt5:mep50 complexed with 5,5-bicyclic inhibitor compound 34
Structure deposition date
2020-10-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
100
Peptide accession
Q9BQA1
Residue number A
186
Residue number B
257
Peptide name
Methylosome protein 50

Ligandability

Cysteine 186 of Methylosome protein 50

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 257 of Methylosome protein 50

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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