Bestrophin
Intermolecular
Cysteine 108 and cysteine 189
Cysteine 185 and cysteine 108
Intramolecular
Cysteine 185 and cysteine 221
Cysteine 185 and cysteine 189
Cysteine 69 and cysteine 251
6vx6 C 108 D 189
A redox-regulated disulphide may form between two units of Bestrophin at cysteines 108 and 189.
Details
Redox score ?
62
PDB code
6vx6
Structure name
bestrophin-2 ca2+-bound state (250 nm ca2+)
Structure deposition date
2020-02-21
Thiol separation (Å)
5
Half-sphere exposure sum ?
98
Minimum pKa ?
8
% buried
100
Peptide A name
Bestrophin
Peptide B name
Bestrophin
Peptide A accession
E1BF86
Peptide B accession
E1BF86
Peptide A residue number
108
Peptide B residue number
189
Ligandability
Cysteine 108 of Bestrophin
Cysteine 189 of Bestrophin
6vx9 E 185 D 108
A redox-regulated disulphide may form between two units of Bestrophin at cysteines 185 and 108. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
6vx9
Structure name
bestrophin-2 ca2+- unbound state 1 (egta only)
Structure deposition date
2020-02-21
Thiol separation (Å)
6
Half-sphere exposure sum ?
97
Minimum pKa ?
8
% buried
100
Peptide A name
Bestrophin
Peptide B name
Bestrophin
Peptide A accession
E1BF86
Peptide B accession
E1BF86
Peptide A residue number
185
Peptide B residue number
108
Ligandability
Cysteine 185 of Bestrophin
Cysteine 108 of Bestrophin
6vx5 A 185 A 221
A redox-regulated disulphide may form within Bestrophin between cysteines 185 and 221. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
6vx5
Structure name
bestrophin-2 ca2+- unbound state (250 nm ca2+)
Structure deposition date
2020-02-21
Thiol separation (Å)
6
Half-sphere exposure sum ?
89
Minimum pKa ?
12
% buried
100
Peptide accession
E1BF86
Residue number A
185
Residue number B
221
Peptide name
Bestrophin
Ligandability
Cysteine 185 of Bestrophin
Cysteine 221 of Bestrophin
6vx9 A 185 A 189
A redox-regulated disulphide may form within Bestrophin between cysteines 185 and 189. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
6vx9
Structure name
bestrophin-2 ca2+- unbound state 1 (egta only)
Structure deposition date
2020-02-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
91
Minimum pKa ?
12
% buried
100
Peptide accession
E1BF86
Residue number A
185
Residue number B
189
Peptide name
Bestrophin
Ligandability
Cysteine 185 of Bestrophin
Cysteine 189 of Bestrophin
6vx9 B 69 B 251
A redox-regulated disulphide may form within Bestrophin between cysteines 69 and 251. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
6vx9
Structure name
bestrophin-2 ca2+- unbound state 1 (egta only)
Structure deposition date
2020-02-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
84
Peptide accession
E1BF86
Residue number A
69
Residue number B
251
Peptide name
Bestrophin
Ligandability
Cysteine 69 of Bestrophin
Cysteine 251 of Bestrophin
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