S-arrestin
Intramolecular
Cysteine 129 and cysteine 144
Cysteine 64 and cysteine 129
Cysteine 322 and cysteine 323
Cysteine 322 and cysteine 4
Cysteine 140 and cysteine 222
5dgy C 185 C 187
A redox-regulated disulphide may form within S-arrestin between cysteines 129 and 144 (185 and 187 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
5dgy
Structure name
crystal structure of rhodopsin bound to visual arrestin
Structure deposition date
2015-08-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
101
Minimum pKa ?
12
% buried
nan
Peptide accession
P20443
Residue number A
129
Residue number B
144
Peptide name
S-arrestin
Ligandability
Cysteine 129 of S-arrestin
Cysteine 144 of S-arrestin
5dgy A 1064 A 1129
A redox-regulated disulphide may form within S-arrestin between cysteines 64 and 129 (1064 and 1129 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
25
PDB code
5dgy
Structure name
crystal structure of rhodopsin bound to visual arrestin
Structure deposition date
2015-08-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
100
Peptide accession
P20443
Residue number A
64
Residue number B
129
Peptide name
S-arrestin
Ligandability
Cysteine 64 of S-arrestin
Cysteine 129 of S-arrestin
5w0p A 322 A 323
A redox-regulated disulphide may form within S-arrestin between cysteines 322 and 323.
Details
Redox score ?
nan
PDB code
5w0p
Structure name
crystal structure of rhodopsin bound to visual arrestin determined by x-ray free electron laser
Structure deposition date
2017-05-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
28
Minimum pKa ?
9
% buried
6
Peptide accession
P20443
Residue number A
322
Residue number B
323
Peptide name
S-arrestin
Ligandability
Cysteine 322 of S-arrestin
Cysteine 323 of S-arrestin
Cysteine 322 in protein A could not be asigned to a Uniprot residue.
Cysteine 323 in protein B could not be asigned to a Uniprot residue.
5dgy A 322 A 323
A redox-regulated disulphide may form within S-arrestin between cysteines 322 and 4 (322 and 323 respectively in this structure).
Details
Redox score ?
nan
PDB code
5dgy
Structure name
crystal structure of rhodopsin bound to visual arrestin
Structure deposition date
2015-08-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
21
Minimum pKa ?
9
% buried
0
Peptide accession
P20443
Residue number A
322
Residue number B
4
Peptide name
S-arrestin
Ligandability
Cysteine 322 of S-arrestin
Cysteine 4 of S-arrestin
Cysteine 322 in protein A could not be asigned to a Uniprot residue.
Uncertain whether structure cysteine 323 has been assigned to correct residue.
5w0p A 140 A 222
A redox-regulated disulphide may form within S-arrestin between cysteines 140 and 222.
Details
Redox score ?
nan
PDB code
5w0p
Structure name
crystal structure of rhodopsin bound to visual arrestin determined by x-ray free electron laser
Structure deposition date
2017-05-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
58
Peptide accession
P20443
Residue number A
140
Residue number B
222
Peptide name
S-arrestin
Ligandability
Cysteine 140 of S-arrestin
Cysteine 222 of S-arrestin
Cysteine 140 in protein A could not be asigned to a Uniprot residue.
Cysteine 222 in protein B could not be asigned to a Uniprot residue.
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