Guanidinoacetate N-methyltransferase
1p1c A 219 B 219
A redox-regulated disulphide may form between two units of Guanidinoacetate N-methyltransferase at cysteines 220 and 220 (219 and 219 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
1p1c
Structure name
guanidinoacetate methyltransferase with gd ion
Structure deposition date
2003-04-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide A name
Guanidinoacetate N-methyltransferase
Peptide B name
Guanidinoacetate N-methyltransferase
Peptide A accession
P10868
Peptide B accession
P10868
Peptide A residue number
220
Peptide B residue number
220
Ligandability
3orh B 16 C 16
A redox-regulated disulphide may form between two units of Guanidinoacetate N-methyltransferase at cysteines 16 and 16. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
3orh
Structure name
human guanidinoacetate n-methyltransferase with sah
Structure deposition date
2010-09-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
98
Peptide A name
Guanidinoacetate N-methyltransferase
Peptide B name
Guanidinoacetate N-methyltransferase
Peptide A accession
Q14353
Peptide B accession
Q14353
Peptide A residue number
16
Peptide B residue number
16
Ligandability
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