Protein arginine N-methyltransferase 5
Intermolecular
Cysteine 196 and cysteine 622
Cysteine 22 and cysteine 53 of Methylosome protein 50 L
Intramolecular
Cysteine 518 and cysteine 536
Cysteine 599 and cysteine 622
Cysteine 536 and cysteine 599
7m05 E 196 G 622
A redox-regulated disulphide may form between two units of Protein arginine N-methyltransferase 5 at cysteines 196 and 622. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
7m05
Structure name
cryoem structure of prmt5 bound to covalent pbm-site inhibitor brd- 6988
Structure deposition date
2021-03-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
12
% buried
100
Peptide A name
Protein arginine N-methyltransferase 5
Peptide B name
Protein arginine N-methyltransferase 5
Peptide A accession
O14744
Peptide B accession
O14744
Peptide A residue number
196
Peptide B residue number
622
Ligandability
Cysteine 196 of Protein arginine N-methyltransferase 5
Cysteine 622 of Protein arginine N-methyltransferase 5
5fa5 A 22 B 53
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
Cysteine 53 of Methylosome protein 50
6v0o A 518 A 536
A redox-regulated disulphide may form within Protein arginine N-methyltransferase 5 between cysteines 518 and 536.
Details
Redox score ?
74
PDB code
6v0o
Structure name
prmt5 bound to the pbm peptide from picln
Structure deposition date
2019-11-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
7
% buried
77
Peptide accession
O14744
Residue number A
518
Residue number B
536
Peptide name
Protein arginine N-methyltransferase 5
Ligandability
Cysteine 518 of Protein arginine N-methyltransferase 5
Cysteine 536 of Protein arginine N-methyltransferase 5
6k1s A 599 A 622
A redox-regulated disulphide may form within Protein arginine N-methyltransferase 5 between cysteines 599 and 622. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
6k1s
Structure name
discovery of potent and selective covalent protein arginine methyltransferase (prmt5) inhibitors
Structure deposition date
2019-05-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
12
Peptide accession
O14744
Residue number A
599
Residue number B
622
Peptide name
Protein arginine N-methyltransferase 5
Ligandability
Cysteine 599 of Protein arginine N-methyltransferase 5
Cysteine 622 of Protein arginine N-methyltransferase 5
7kib A 536 A 599
A redox-regulated disulphide may form within Protein arginine N-methyltransferase 5 between cysteines 536 and 599. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
7kib
Structure name
prmt5:mep50 complexed with 5,5-bicyclic inhibitor compound 4
Structure deposition date
2020-10-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
7
% buried
38
Peptide accession
O14744
Residue number A
536
Residue number B
599
Peptide name
Protein arginine N-methyltransferase 5
Ligandability
Cysteine 536 of Protein arginine N-methyltransferase 5
Cysteine 599 of Protein arginine N-methyltransferase 5
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