Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Intermolecular
Cysteine 25 and cysteine 36 of Guanine nucleotide-binding protein G(T) subunit gamma-T1 L
Cysteine 25 and cysteine 37 of Guanine nucleotide-binding protein G(T) subunit gamma-T1 L
Cysteine 214 of Guanine nucleotide-binding protein G(i) subunit alpha-1 and cysteine 204
Intramolecular
Cysteine 121 and cysteine 149 L
Cysteine 148 and cysteine 149
Cysteine 103 and cysteine 114
Cysteine 103 and cysteine 149
Cysteine 114 and cysteine 149
Cysteine 114 and cysteine 121 L
Cysteine 233 and cysteine 317
More...Cysteine 103 and cysteine 317
Cysteine 103 and cysteine 121 L
Cysteine 166 and cysteine 218
Cysteine 103 and cysteine 148
Cysteine 148 and cysteine 233
Cysteine 271 and cysteine 294 L
Cysteine 148 and cysteine 166
Cysteine 148 and cysteine 317
Cysteine 250 and cysteine 294
Cysteine 250 and cysteine 271 L
Cysteine 233 and cysteine 250
Cysteine 149 and cysteine 166
Cysteine 294 and cysteine 317
Cysteine 121 and cysteine 148 L
1got B 25 G 36
A redox-regulated disulphide may form between cysteine 25 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 and cysteine 36 of Guanine nucleotide-binding protein G(T) subunit gamma-T1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
1got
Structure name
heterotrimeric complex of a gt-alpha/gi-alpha chimera and the gt-beta-gamma subunits
Structure deposition date
1996-08-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
32
Peptide A name
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Peptide B name
Guanine nucleotide-binding protein G(T) subunit gamma-T1
Peptide A accession
P62871
Peptide B accession
P02698
Peptide A residue number
25
Peptide B residue number
36
Ligandability
Cysteine 25 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Cysteine 36 of Guanine nucleotide-binding protein G(T) subunit gamma-T1
6oy9 B 25 G 37
A redox-regulated disulphide may form between cysteine 25 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 and cysteine 37 of Guanine nucleotide-binding protein G(T) subunit gamma-T1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
6oy9
Structure name
structure of the rhodopsin-transducin complex
Structure deposition date
2019-05-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
8
% buried
38
Peptide A name
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Peptide B name
Guanine nucleotide-binding protein G(T) subunit gamma-T1
Peptide A accession
P62871
Peptide B accession
P02698
Peptide A residue number
25
Peptide B residue number
37
Ligandability
Cysteine 25 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Cysteine 37 of Guanine nucleotide-binding protein G(T) subunit gamma-T1
6qno A 214 B 204
A redox-regulated disulphide may form between cysteine 214 of Guanine nucleotide-binding protein G(i) subunit alpha-1 and cysteine 204 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
6qno
Structure name
rhodopsin-gi protein complex
Structure deposition date
2019-02-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
85
Peptide A name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Peptide B name
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Peptide A accession
P63096
Peptide B accession
P62871
Peptide A residue number
214
Peptide B residue number
204
Ligandability
Cysteine 214 of Guanine nucleotide-binding protein G(i) subunit alpha-1
Cysteine 204 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
5he3 B 121 B 149
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 between cysteines 121 and 149.
Details
Redox score ?
66
PDB code
5he3
Structure name
bovine grk2 in complex with gbetagamma subunits and ccg224411
Structure deposition date
2016-01-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
100
Minimum pKa ?
8
% buried
100
Peptide accession
P62873
Residue number A
121
Residue number B
149
Peptide name
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Ligandability
Cysteine 121 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Cysteine 149 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
5tdh B 148 B 149
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 between cysteines 148 and 149. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
5tdh
Structure name
the crystal structure of the dominant negative mutant g protein alpha(i)-1-beta-1-gamma-2 g203a/a326s
Structure deposition date
2016-09-19
Thiol separation (Å)
6
Half-sphere exposure sum ?
97
Minimum pKa ?
8
% buried
100
Peptide accession
P54311
Residue number A
148
Residue number B
149
Peptide name
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Ligandability
Cysteine 148 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Cysteine 149 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
6b20 A 103 A 114
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 between cysteines 103 and 114. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
6b20
Structure name
crystal structure of a complex between g protein beta gamma dimer and an inhibitory nanobody regulator
Structure deposition date
2017-09-19
Thiol separation (Å)
6
Half-sphere exposure sum ?
102
Minimum pKa ?
nan
% buried
nan
Peptide accession
P62871
Residue number A
103
Residue number B
114
Peptide name
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Ligandability
Cysteine 103 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Cysteine 114 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
5tdh J 103 J 149
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 between cysteines 103 and 149. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
5tdh
Structure name
the crystal structure of the dominant negative mutant g protein alpha(i)-1-beta-1-gamma-2 g203a/a326s
Structure deposition date
2016-09-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
91
Minimum pKa ?
8
% buried
100
Peptide accession
P54311
Residue number A
103
Residue number B
149
Peptide name
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Ligandability
Cysteine 103 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Cysteine 149 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
6rmv A 114 A 149
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 between cysteines 114 and 149. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
6rmv
Structure name
the crystal structure of a trp channel peptide bound to a g protein beta gamma heterodimer
Structure deposition date
2019-05-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
101
Minimum pKa ?
8
% buried
100
Peptide accession
P62874
Residue number A
114
Residue number B
149
Peptide name
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Ligandability
Cysteine 114 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Cysteine 149 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
3sn6 B 114 B 121
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 between cysteines 114 and 121. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
3sn6
Structure name
crystal structure of the beta2 adrenergic receptor-gs protein complex
Structure deposition date
2011-06-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
107
Minimum pKa ?
13
% buried
100
Peptide accession
P54311
Residue number A
114
Residue number B
121
Peptide name
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Ligandability
Cysteine 114 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Cysteine 121 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
6lpb B 233 B 317
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 between cysteines 233 and 317. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
6lpb
Structure name
cryo-em structure of the human pac1 receptor coupled to an engineered heterotrimeric g protein
Structure deposition date
2020-01-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
95
Minimum pKa ?
9
% buried
100
Peptide accession
P54311
Residue number A
233
Residue number B
317
Peptide name
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Ligandability
Cysteine 233 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Cysteine 317 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
5tdh J 103 J 317
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 between cysteines 103 and 317. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
5tdh
Structure name
the crystal structure of the dominant negative mutant g protein alpha(i)-1-beta-1-gamma-2 g203a/a326s
Structure deposition date
2016-09-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
98
Minimum pKa ?
12
% buried
100
Peptide accession
P54311
Residue number A
103
Residue number B
317
Peptide name
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Ligandability
Cysteine 103 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Cysteine 317 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
6cmo B 103 B 121
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 between cysteines 103 and 121. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
6cmo
Structure name
rhodopsin-gi complex
Structure deposition date
2018-03-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
85
Minimum pKa ?
9
% buried
100
Peptide accession
P54311
Residue number A
103
Residue number B
121
Peptide name
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Ligandability
Cysteine 103 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Cysteine 121 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
7joz B 166 B 218
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 between cysteines 166 and 218. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
7joz
Structure name
crystal structure of dopamine d1 receptor in complex with g protein and a non-catechol agonist
Structure deposition date
2020-08-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
11
% buried
78
Peptide accession
P62873
Residue number A
166
Residue number B
218
Peptide name
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Ligandability
Cysteine 166 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Cysteine 218 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
5ukk B 103 B 148
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 between cysteines 103 and 148. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
5ukk
Structure name
human grk2 in complex with human g-beta-gamma subunits and ccg211998 (14ak)
Structure deposition date
2017-01-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
101
Minimum pKa ?
9
% buried
100
Peptide accession
P62873
Residue number A
103
Residue number B
148
Peptide name
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Ligandability
Cysteine 103 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Cysteine 148 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
7ew4 B 148 B 233
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 between cysteines 148 and 233. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
7ew4
Structure name
cryo-em structure of cym-5541-bound sphingosine 1-phosphate receptor 3 in complex with gi protein
Structure deposition date
2021-05-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
94
Minimum pKa ?
10
% buried
100
Peptide accession
P62873
Residue number A
148
Residue number B
233
Peptide name
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Ligandability
Cysteine 148 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Cysteine 233 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
8f7r B 271 B 294
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 between cysteines 271 and 294. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
8f7r
Structure name
gi bound mu-opioid receptor in complex with endomorphin
Structure deposition date
2022-11-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
70
Peptide accession
P54311
Residue number A
271
Residue number B
294
Peptide name
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Ligandability
Cysteine 271 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Cysteine 294 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
6rmv A 148 A 166
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 between cysteines 148 and 166. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
6rmv
Structure name
the crystal structure of a trp channel peptide bound to a g protein beta gamma heterodimer
Structure deposition date
2019-05-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
103
Minimum pKa ?
10
% buried
100
Peptide accession
P62874
Residue number A
148
Residue number B
166
Peptide name
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Ligandability
Cysteine 148 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Cysteine 166 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
1xhm A 148 A 317
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 between cysteines 148 and 317. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
1xhm
Structure name
the crystal structure of a biologically active peptide (sigk) bound to a g protein beta:gamma heterodimer
Structure deposition date
2004-09-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
105
Minimum pKa ?
10
% buried
100
Peptide accession
P62871
Residue number A
148
Residue number B
317
Peptide name
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Ligandability
Cysteine 148 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Cysteine 317 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
3uzs B 250 B 294
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 between cysteines 250 and 294. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
3uzs
Structure name
structure of the c13
Structure deposition date
2011-12-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
92
Minimum pKa ?
12
% buried
100
Peptide accession
P62871
Residue number A
250
Residue number B
294
Peptide name
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Ligandability
Cysteine 250 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Cysteine 294 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
7o7f B 250 B 271
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 between cysteines 250 and 271. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
7o7f
Structure name
structural basis of the activation of the cc chemokine receptor 5 by a chemokine agonist
Structure deposition date
2021-04-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
80
Minimum pKa ?
11
% buried
74
Peptide accession
P62871
Residue number A
250
Residue number B
271
Peptide name
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Ligandability
Cysteine 250 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Cysteine 271 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
7d3s B 233 B 250
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 between cysteines 233 and 250. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
7d3s
Structure name
human secr in complex with an engineered gs heterotrimer
Structure deposition date
2020-09-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
97
Minimum pKa ?
12
% buried
100
Peptide accession
P54311
Residue number A
233
Residue number B
250
Peptide name
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Ligandability
Cysteine 233 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Cysteine 250 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
6gdg B 149 B 166
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 between cysteines 149 and 166. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
29
PDB code
6gdg
Structure name
cryo-em structure of the adenosine a2a receptor bound to a minigs heterotrimer
Structure deposition date
2018-04-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
98
Minimum pKa ?
12
% buried
nan
Peptide accession
P62873
Residue number A
149
Residue number B
166
Peptide name
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Ligandability
Cysteine 149 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Cysteine 166 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
6rmv A 294 A 317
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 between cysteines 294 and 317. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
28
PDB code
6rmv
Structure name
the crystal structure of a trp channel peptide bound to a g protein beta gamma heterodimer
Structure deposition date
2019-05-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
95
Minimum pKa ?
12
% buried
100
Peptide accession
P62874
Residue number A
294
Residue number B
317
Peptide name
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Ligandability
Cysteine 294 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Cysteine 317 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
5tdh J 121 J 148
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 between cysteines 121 and 148. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
27
PDB code
5tdh
Structure name
the crystal structure of the dominant negative mutant g protein alpha(i)-1-beta-1-gamma-2 g203a/a326s
Structure deposition date
2016-09-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
98
Minimum pKa ?
11
% buried
100
Peptide accession
P54311
Residue number A
121
Residue number B
148
Peptide name
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Ligandability
Cysteine 121 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Cysteine 148 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
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