Guanine nucleotide-binding protein G(i) subunit alpha-1
Intermolecular
Cysteine 214 and cysteine 214
Cysteine 351 and cysteine 133 of Muscarinic acetylcholine receptor M4
Cysteine 351 and cysteine 134 of Cannabinoid receptor 2
Cysteine 351 and cysteine 151 of Neuropeptide Y receptor type 2
Cysteine 126 of fMet-Leu-Phe receptor and cysteine 351
Cysteine 126 of N-formyl peptide receptor 2 and cysteine 351
Cysteine 351 and cysteine 66 of G-protein coupled receptor homolog US28
Cysteine 351 and cysteine 456 of Muscarinic acetylcholine receptor M4
Cysteine 351 and cysteine 122 of Synembryn
Cysteine 171 of Neurotensin receptor type 1 and cysteine 351
More...Cysteine 305 and cysteine 305
Cysteine 140 of Rhodopsin and cysteine 351
Cysteine 75 of C-C chemokine receptor type 2 and cysteine 351
Cysteine 351 and cysteine 626 of Adhesion G-protein coupled receptor F1
Cysteine 351 and cysteine 63 of N-formyl peptide receptor 2
Cysteine 214 and cysteine 204 of Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Cysteine 351 and cysteine 123 of 5-hydroxytryptamine receptor 4
Intramolecular
Cysteine 47 and cysteine 325
Cysteine 224 and cysteine 224
Cysteine 56 and cysteine 333
Cysteine 47 and cysteine 224
2zjz A 214 B 214
A redox-regulated disulphide may form between two units of Guanine nucleotide-binding protein G(i) subunit alpha-1 at cysteines 214 and 214.
Details
Redox score ?
85
PDB code
2zjz
Structure name
structure of the k349p mutant of gi alpha 1 subunit bound to gdp
Structure deposition date
2008-03-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide A name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Peptide B name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Peptide A accession
P10824
Peptide B accession
P10824
Peptide A residue number
214
Peptide B residue number
214
Ligandability
7v6a A 351 R 133
A redox-regulated disulphide may form between cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1 and cysteine 133 of Muscarinic acetylcholine receptor M4.
Details
Redox score ?
72
PDB code
7v6a
Structure name
cry-em structure of m4-c110-g protein complex
Structure deposition date
2021-08-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
8
% buried
84
Peptide A name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Peptide B name
Muscarinic acetylcholine receptor M4
Peptide A accession
P63096
Peptide B accession
P08173
Peptide A residue number
351
Peptide B residue number
133
Ligandability
Cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1
Cysteine 133 of Muscarinic acetylcholine receptor M4
6kpf A 351 R 134
A redox-regulated disulphide may form between cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1 and cysteine 134 of Cannabinoid receptor 2.
Details
Redox score ?
71
PDB code
6kpf
Structure name
cryo-em structure of a class a gpcr with g protein complex
Structure deposition date
2019-08-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
80
Minimum pKa ?
8
% buried
100
Peptide A name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Peptide B name
Cannabinoid receptor 2
Peptide A accession
P63096
Peptide B accession
P34972
Peptide A residue number
351
Peptide B residue number
134
Ligandability
Cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1
Cysteine 134 of Cannabinoid receptor 2
7x9b A 351 R 151
A redox-regulated disulphide may form between cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1 and cysteine 151 of Neuropeptide Y receptor type 2.
Details
Redox score ?
71
PDB code
7x9b
Structure name
cryo-em structure of neuropeptide y y2 receptor in complex with npy and gi
Structure deposition date
2022-03-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
9
% buried
86
Peptide A name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Peptide B name
Neuropeptide Y receptor type 2
Peptide A accession
P63096
Peptide B accession
P49146
Peptide A residue number
351
Peptide B residue number
151
Ligandability
Cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1
Cysteine 151 of Neuropeptide Y receptor type 2
7vfx R 126 A 351
A redox-regulated disulphide may form between cysteine 126 of fMet-Leu-Phe receptor and cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
7vfx
Structure name
the structure of formyl peptide receptor 1 in complex with gi and peptide agonist fmifl
Structure deposition date
2021-09-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
90
Peptide A name
fMet-Leu-Phe receptor
Peptide B name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Peptide A accession
P21462
Peptide B accession
P63096
Peptide A residue number
126
Peptide B residue number
351
Ligandability
Cysteine 126 of fMet-Leu-Phe receptor
Cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1
6omm R 126 A 351
A redox-regulated disulphide may form between cysteine 126 of N-formyl peptide receptor 2 and cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
6omm
Structure name
cryo-em structure of formyl peptide receptor 2/lipoxin a4 receptor in complex with gi
Structure deposition date
2019-04-19
Thiol separation (Å)
5
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
100
Peptide A name
N-formyl peptide receptor 2
Peptide B name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Peptide A accession
P25090
Peptide B accession
P63096
Peptide A residue number
126
Peptide B residue number
351
Ligandability
Cysteine 126 of N-formyl peptide receptor 2
Cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1
7rkm A 351 R 66
A redox-regulated disulphide may form between cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1 and cysteine 66 of G-protein coupled receptor homolog US28. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
7rkm
Structure name
structure of cx3cl1-us28-gi-scfv16 in c-state
Structure deposition date
2021-07-22
Thiol separation (Å)
6
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
100
Peptide A name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Peptide B name
G-protein coupled receptor homolog US28
Peptide A accession
P63096
Peptide B accession
P69332
Peptide A residue number
351
Peptide B residue number
66
Ligandability
Cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1
Cysteine 66 of G-protein coupled receptor homolog US28
7v69 A 351 R 456
A redox-regulated disulphide may form between cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1 and cysteine 456 of Muscarinic acetylcholine receptor M4. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
7v69
Structure name
cryo-em structure of a class a gpcr-g protein complex
Structure deposition date
2021-08-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
79
Peptide A name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Peptide B name
Muscarinic acetylcholine receptor M4
Peptide A accession
P63096
Peptide B accession
P08173
Peptide A residue number
351
Peptide B residue number
456
Ligandability
Cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1
Cysteine 456 of Muscarinic acetylcholine receptor M4
6tyl G 351 F 122
A redox-regulated disulphide may form between cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1 and cysteine 122 of Synembryn. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
6tyl
Structure name
crystal structure of mammalian ric-8a:galpha(i):nanobody complex
Structure deposition date
2019-08-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
84
Peptide A name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Peptide B name
Synembryn
Peptide A accession
P10824
Peptide B accession
B1H241
Peptide A residue number
351
Peptide B residue number
122
Ligandability
Cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1
Cysteine 122 of Synembryn
6osa R 171 A 351
A redox-regulated disulphide may form between cysteine 171 of Neurotensin receptor type 1 and cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
6osa
Structure name
human neurotensin receptor 1 (hntsr1) - gi1 protein complex in non- canonical conformation (nc state)
Structure deposition date
2019-05-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
66
Peptide A name
Neurotensin receptor type 1
Peptide B name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Peptide A accession
P30989
Peptide B accession
P63096
Peptide A residue number
171
Peptide B residue number
351
Ligandability
Cysteine 171 of Neurotensin receptor type 1
Cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1
2xns A 305 B 305
A redox-regulated disulphide may form between two units of Guanine nucleotide-binding protein G(i) subunit alpha-1 at cysteines 305 and 305. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
2xns
Structure name
crystal structure of human g alpha i1 bound to a designed helical peptide derived from the goloco motif of rgs14
Structure deposition date
2010-08-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
48
Minimum pKa ?
11
% buried
56
Peptide A name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Peptide B name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Peptide A accession
P63096
Peptide B accession
P63096
Peptide A residue number
305
Peptide B residue number
305
Ligandability
6cmo R 140 A 351
A redox-regulated disulphide may form between cysteine 140 of Rhodopsin and cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1. 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)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
11
% buried
64
Peptide A name
Rhodopsin
Peptide B name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Peptide A accession
P08100
Peptide B accession
P63096
Peptide A residue number
140
Peptide B residue number
351
Ligandability
Cysteine 140 of Rhodopsin
Cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1
7xa3 R 75 A 351
A redox-regulated disulphide may form between cysteine 75 of C-C chemokine receptor type 2 and cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
7xa3
Structure name
cryo-em structure of the ccl2 bound ccr2-gi complex
Structure deposition date
2022-03-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
84
Peptide A name
C-C chemokine receptor type 2
Peptide B name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Peptide A accession
P41597
Peptide B accession
P63096
Peptide A residue number
75
Peptide B residue number
351
Ligandability
Cysteine 75 of C-C chemokine receptor type 2
Cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1
7wu5 A 351 R 626
A redox-regulated disulphide may form between cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1 and cysteine 626 of Adhesion G-protein coupled receptor F1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
7wu5
Structure name
cryo-em structure of the adhesion gpcr adgrf1(h565a/t567a) in complex with minigi
Structure deposition date
2022-02-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
100
Peptide A name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Peptide B name
Adhesion G-protein coupled receptor F1
Peptide A accession
P63096
Peptide B accession
Q5T601
Peptide A residue number
351
Peptide B residue number
626
Ligandability
Cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1
Cysteine 626 of Adhesion G-protein coupled receptor F1
7t6s A 351 R 63
A redox-regulated disulphide may form between cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1 and cysteine 63 of N-formyl peptide receptor 2. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
7t6s
Structure name
molecular recognition of formylpeptides and diverse agonists by the formylpeptide receptors fpr1 and fpr2
Structure deposition date
2021-12-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
11
% buried
96
Peptide A name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Peptide B name
N-formyl peptide receptor 2
Peptide A accession
P63096
Peptide B accession
P25090
Peptide A residue number
351
Peptide B residue number
63
Ligandability
Cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1
Cysteine 63 of N-formyl peptide receptor 2
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
7xta A 351 R 122
A redox-regulated disulphide may form between cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1 and cysteine 123 of 5-hydroxytryptamine receptor 4 (351 and 122 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
7xta
Structure name
serotonin 4 (5-ht4) receptor-gi-scfv16 complex
Structure deposition date
2022-05-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
10
% buried
74
Peptide A name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Peptide B name
5-hydroxytryptamine receptor 4
Peptide A accession
P63096
Peptide B accession
Q13639
Peptide A residue number
351
Peptide B residue number
123
Ligandability
Cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1
Cysteine 123 of 5-hydroxytryptamine receptor 4
7xmt A 47 A 325
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(i) subunit alpha-1 between cysteines 47 and 325. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
7xmt
Structure name
cryoem structure of somatostatin receptor 4 (sstr4) with gi1 and j- 2156
Structure deposition date
2022-04-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
51
Minimum pKa ?
8
% buried
5
Peptide accession
P63096
Residue number A
47
Residue number B
325
Peptide name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Ligandability
Cysteine 47 of Guanine nucleotide-binding protein G(i) subunit alpha-1
Cysteine 325 of Guanine nucleotide-binding protein G(i) subunit alpha-1
Cysteine 47 in protein A could not be asigned to a Uniprot residue.
4pao A 224 A 336
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(i) subunit alpha-1 between cysteines 224 and 224 (224 and 336 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
4pao
Structure name
a conserved phenylalanine as relay between the 5 helix and the gdp binding region of heterotrimeric g protein
Structure deposition date
2014-04-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
100
Peptide accession
P10824
Residue number A
224
Residue number B
224
Peptide name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Ligandability
Cysteine 224 of Guanine nucleotide-binding protein G(i) subunit alpha-1
Cysteine 224 of Guanine nucleotide-binding protein G(i) subunit alpha-1
3d7m A 56 A 333
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(i) subunit alpha-1 between cysteines 56 and 333.
Details
Redox score ?
nan
PDB code
3d7m
Structure name
crystal structure of the g protein fast-exchange double mutant i56c/q333c
Structure deposition date
2008-05-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10824
Residue number A
56
Residue number B
333
Peptide name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Ligandability
Cysteine 56 of Guanine nucleotide-binding protein G(i) subunit alpha-1
Cysteine 333 of Guanine nucleotide-binding protein G(i) subunit alpha-1
Cysteine 56 in protein A could not be asigned to a Uniprot residue.
Cysteine 333 in protein B could not be asigned to a Uniprot residue.
7f1s A 47 A 224
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(i) subunit alpha-1 between cysteines 47 and 224.
Details
Redox score ?
nan
PDB code
7f1s
Structure name
cryo-em structure of the apo chemokine receptor ccr5 in complex with gi
Structure deposition date
2021-06-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
69
Minimum pKa ?
9
% buried
65
Peptide accession
P63096
Residue number A
47
Residue number B
224
Peptide name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Ligandability
Cysteine 47 of Guanine nucleotide-binding protein G(i) subunit alpha-1
Cysteine 224 of Guanine nucleotide-binding protein G(i) subunit alpha-1
Cysteine 47 in protein A could not be asigned to a Uniprot residue.
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