Synembryn-A
Intermolecular
Cysteine 122 and cysteine 351 of Guanine nucleotide-binding protein G(t) subunit alpha-2
Intramolecular
Cysteine 120 and cysteine 122
6n85 B 122 M 392
A redox-regulated disulphide may form between cysteine 122 of Synembryn-A and cysteine 351 of Guanine nucleotide-binding protein G(t) subunit alpha-2 (122 and 392 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
6n85
Structure name
resistance to inhibitors of cholinesterase 8a (ric8a) protein in complex with mbp-tagged transducin-alpha residues 327-350
Structure deposition date
2018-11-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
86
Peptide A name
Synembryn-A
Peptide B name
Guanine nucleotide-binding protein G(t) subunit alpha-2
Peptide A accession
Q5E9J8
Peptide B accession
P19087
Peptide A residue number
122
Peptide B residue number
351
Ligandability
Cysteine 122 of Synembryn-A
Cysteine 351 of Guanine nucleotide-binding protein G(t) subunit alpha-2
6n86 B 120 B 122
A redox-regulated disulphide may form within Synembryn-A between cysteines 120 and 122. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
25
PDB code
6n86
Structure name
resistance to inhibitors of cholinesterase 8a (ric8a) protein
Structure deposition date
2018-11-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
13
% buried
100
Peptide accession
Q5E9J8
Residue number A
120
Residue number B
122
Peptide name
Synembryn-A
Ligandability
Cysteine 120 of Synembryn-A
Cysteine 122 of Synembryn-A
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