Phenylethanolamine N-methyltransferase
Intermolecular
Cysteine 139 and cysteine 48
Cysteine 48 and cysteine 131
Intramolecular
Cysteine 131 and cysteine 139
Cysteine 91 and cysteine 131
4mq4 A 139 B 48
A redox-regulated disulphide may form between two units of Phenylethanolamine N-methyltransferase at cysteines 139 and 48.
Details
Redox score ?
74
PDB code
4mq4
Structure name
crystal structure of hpnmt in complex with bisubstrate inhibitor n-(3- ((((2s,3s,4r,5r)-5-(6-amino-9h-purin-9-yl)-3,4- dihydroxytetrahydrofuran-2-yl)methyl)thio)propyl)-1,2,3,4- tetrahydroisoquinoline-3-carboxamide
Structure deposition date
2013-09-15
Thiol separation (Å)
3
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
48
Peptide A name
Phenylethanolamine N-methyltransferase
Peptide B name
Phenylethanolamine N-methyltransferase
Peptide A accession
P11086
Peptide B accession
P11086
Peptide A residue number
139
Peptide B residue number
48
Ligandability
Cysteine 139 of Phenylethanolamine N-methyltransferase
Cysteine 48 of Phenylethanolamine N-methyltransferase
4mq4 A 48 B 131
A redox-regulated disulphide may form between two units of Phenylethanolamine N-methyltransferase at cysteines 48 and 131. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
4mq4
Structure name
crystal structure of hpnmt in complex with bisubstrate inhibitor n-(3- ((((2s,3s,4r,5r)-5-(6-amino-9h-purin-9-yl)-3,4- dihydroxytetrahydrofuran-2-yl)methyl)thio)propyl)-1,2,3,4- tetrahydroisoquinoline-3-carboxamide
Structure deposition date
2013-09-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
13
% buried
64
Peptide A name
Phenylethanolamine N-methyltransferase
Peptide B name
Phenylethanolamine N-methyltransferase
Peptide A accession
P11086
Peptide B accession
P11086
Peptide A residue number
48
Peptide B residue number
131
Ligandability
Cysteine 48 of Phenylethanolamine N-methyltransferase
Cysteine 131 of Phenylethanolamine N-methyltransferase
7twu B 131 B 139
A redox-regulated disulphide may form within Phenylethanolamine N-methyltransferase between cysteines 131 and 139. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
7twu
Structure name
crystal structure of human phenylethanolamine n-methyltransferase (pnmt) in complex with (2s)-2-amino-4-(((5-(6-amino-9h-purin-9-yl)-3, 4-dihydroxytetrahydrofuran-2-yl)methyl)(4-(7,8-dichloro-1,2,3,4- tetrahydroisoquinolin-4-yl)butyl)amino)butanoic acid and adohcy (sah)
Structure deposition date
2022-02-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
18
Peptide accession
P11086
Residue number A
131
Residue number B
139
Peptide name
Phenylethanolamine N-methyltransferase
Ligandability
Cysteine 131 of Phenylethanolamine N-methyltransferase
Cysteine 139 of Phenylethanolamine N-methyltransferase
3hca B 91 B 131
A redox-regulated disulphide may form within Phenylethanolamine N-methyltransferase between cysteines 91 and 131. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
3hca
Structure name
crystal structure of e185q hpnmt in complex with octopamine and adohcy
Structure deposition date
2009-05-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
92
Peptide accession
P11086
Residue number A
91
Residue number B
131
Peptide name
Phenylethanolamine N-methyltransferase
Ligandability
Cysteine 91 of Phenylethanolamine N-methyltransferase
Cysteine 131 of Phenylethanolamine N-methyltransferase
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