Regulator of G-protein signaling 3
Intermolecular
Cysteine 315 and cysteine 315
Cysteine 314 and cysteine 314
Cysteine 315 and cysteine 354
Cysteine 354 and cysteine 314
Intramolecular
Cysteine 33 and cysteine 73
Cysteine 314 and cysteine 315
Cysteine 170 and cysteine 196
Cysteine 1106 and cysteine 1159
2f5y A 34 B 34
A redox-regulated disulphide may form between two units of Regulator of G-protein signaling 3 at cysteines 315 and 315 (34 and 34 respectively in this structure).
Details
Redox score ?
75
PDB code
2f5y
Structure name
crystal structure of the pdz domain from human rgs-3
Structure deposition date
2005-11-28
Thiol separation (Å)
3
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide A name
Regulator of G-protein signaling 3
Peptide B name
Regulator of G-protein signaling 3
Peptide A accession
P49796
Peptide B accession
P49796
Peptide A residue number
315
Peptide B residue number
315
Ligandability
2f5y A 33 B 33
A redox-regulated disulphide may form between two units of Regulator of G-protein signaling 3 at cysteines 314 and 314 (33 and 33 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
2f5y
Structure name
crystal structure of the pdz domain from human rgs-3
Structure deposition date
2005-11-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide A name
Regulator of G-protein signaling 3
Peptide B name
Regulator of G-protein signaling 3
Peptide A accession
P49796
Peptide B accession
P49796
Peptide A residue number
314
Peptide B residue number
314
Ligandability
2f5y A 34 B 73
A redox-regulated disulphide may form between two units of Regulator of G-protein signaling 3 at cysteines 315 and 354 (34 and 73 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
2f5y
Structure name
crystal structure of the pdz domain from human rgs-3
Structure deposition date
2005-11-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
nan
Peptide A name
Regulator of G-protein signaling 3
Peptide B name
Regulator of G-protein signaling 3
Peptide A accession
P49796
Peptide B accession
P49796
Peptide A residue number
315
Peptide B residue number
354
Ligandability
Cysteine 315 of Regulator of G-protein signaling 3
Cysteine 354 of Regulator of G-protein signaling 3
2f5y A 73 B 33
A redox-regulated disulphide may form between two units of Regulator of G-protein signaling 3 at cysteines 354 and 314 (73 and 33 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
2f5y
Structure name
crystal structure of the pdz domain from human rgs-3
Structure deposition date
2005-11-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
nan
Peptide A name
Regulator of G-protein signaling 3
Peptide B name
Regulator of G-protein signaling 3
Peptide A accession
P49796
Peptide B accession
P49796
Peptide A residue number
354
Peptide B residue number
314
Ligandability
Cysteine 354 of Regulator of G-protein signaling 3
Cysteine 314 of Regulator of G-protein signaling 3
1whd A 33 A 73
A redox-regulated disulphide may form within Regulator of G-protein signaling 3 between cysteines 33 and 73.
Details
Redox score ?
69
PDB code
1whd
Structure name
solution structure of the pdz domain of rgs3
Structure deposition date
2004-05-28
Thiol separation (Å)
5
Half-sphere exposure sum ?
50
Minimum pKa ?
9
% buried
0
Peptide accession
Q9DC04
Residue number A
33
Residue number B
73
Peptide name
Regulator of G-protein signaling 3
Ligandability
Cysteine 33 of Regulator of G-protein signaling 3
Cysteine 73 of Regulator of G-protein signaling 3
2f5y A 33 A 34
A redox-regulated disulphide may form within Regulator of G-protein signaling 3 between cysteines 314 and 315 (33 and 34 respectively in this structure).
Details
Redox score ?
64
PDB code
2f5y
Structure name
crystal structure of the pdz domain from human rgs-3
Structure deposition date
2005-11-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P49796
Residue number A
314
Residue number B
315
Peptide name
Regulator of G-protein signaling 3
Ligandability
Cysteine 314 of Regulator of G-protein signaling 3
Cysteine 315 of Regulator of G-protein signaling 3
3fbk B 66 B 92
A redox-regulated disulphide may form within Regulator of G-protein signaling 3 between cysteines 170 and 196 (66 and 92 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
3fbk
Structure name
crystal structure of the c2 domain of the human regulator of g-protein signaling 3 isoform 6 (rgp3), northeast structural genomics consortium target hr5550a
Structure deposition date
2008-11-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
20
Peptide accession
P49796
Residue number A
170
Residue number B
196
Peptide name
Regulator of G-protein signaling 3
Ligandability
Cysteine 170 of Regulator of G-protein signaling 3
Cysteine 196 of Regulator of G-protein signaling 3
2oj4 A 44 A 97
A redox-regulated disulphide may form within Regulator of G-protein signaling 3 between cysteines 1106 and 1159 (44 and 97 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
2oj4
Structure name
crystal structure of rgs3 rgs domain
Structure deposition date
2007-01-12
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
68
Peptide accession
P49796
Residue number A
1106
Residue number B
1159
Peptide name
Regulator of G-protein signaling 3
Ligandability
Cysteine 1106 of Regulator of G-protein signaling 3
Cysteine 1159 of Regulator of G-protein signaling 3
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