Adhesion G protein-coupled receptor L3
Intermolecular
Cysteine 191 and cysteine 191
Intramolecular
Cysteine 78 and cysteine 110
Cysteine 91 and cysteine 97
Cysteine 927 and cysteine 999
Cysteine 36 and cysteine 66
Cysteine 113 and cysteine 191
Cysteine 882 and cysteine 904
Cysteine 203 and cysteine 385
Cysteine 963 and cysteine 1192
Cysteine 959 and cysteine 963
More...Cysteine 985 and cysteine 1192
Cysteine 959 and cysteine 1192
Cysteine 963 and cysteine 968
Cysteine 113 and cysteine 165
Cysteine 113 and cysteine 159
Cysteine 968 and cysteine 985
Cysteine 959 and cysteine 985
Cysteine 1152 and cysteine 1192
Cysteine 963 and cysteine 1152
Cysteine 904 and cysteine 1062
5ftt C 191 G 191
A redox-regulated disulphide may form between two units of Adhesion G protein-coupled receptor L3 at cysteines 191 and 191. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
5ftt
Structure name
octameric complex of latrophilin 3 (lec, olf) , unc5d (ig, ig2, tsp1) and flrt2 (lrr)
Structure deposition date
2016-01-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide A name
Adhesion G protein-coupled receptor L3
Peptide B name
Adhesion G protein-coupled receptor L3
Peptide A accession
Q80TS3
Peptide B accession
Q80TS3
Peptide A residue number
191
Peptide B residue number
191
Ligandability
8djg F 78 F 110
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor L3 between cysteines 78 and 110.
Details
Redox score ?
88
PDB code
8djg
Structure name
adgrl3-lectin domain in complex with an activating synthetic antibody fragment
Structure deposition date
2022-06-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9HAR2
Residue number A
78
Residue number B
110
Peptide name
Adhesion G protein-coupled receptor L3
Ligandability
Cysteine 78 of Adhesion G protein-coupled receptor L3
Cysteine 110 of Adhesion G protein-coupled receptor L3
8djg F 91 F 97
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor L3 between cysteines 91 and 97.
Details
Redox score ?
86
PDB code
8djg
Structure name
adgrl3-lectin domain in complex with an activating synthetic antibody fragment
Structure deposition date
2022-06-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9HAR2
Residue number A
91
Residue number B
97
Peptide name
Adhesion G protein-coupled receptor L3
Ligandability
Cysteine 91 of Adhesion G protein-coupled receptor L3
Cysteine 97 of Adhesion G protein-coupled receptor L3
7sf7 A 927 A 999
A redox-regulated disulphide may form within Isoform 1 of Adhesion G protein-coupled receptor L3 between cysteines 927 and 999.
Details
Redox score ?
86
PDB code
7sf7
Structure name
lphn3 (adgrl3) 7tm domain bound to tethered agonist in complex with g protein heterotrimer
Structure deposition date
2021-10-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9HAR2-1
Residue number A
927
Residue number B
999
Peptide name
Isoform 1 of Adhesion G protein-coupled receptor L3
Ligandability
Cysteine 927 of Isoform 1 of Adhesion G protein-coupled receptor L3
Cysteine 999 of Isoform 1 of Adhesion G protein-coupled receptor L3
8djg F 36 F 66
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor L3 between cysteines 36 and 66.
Details
Redox score ?
82
PDB code
8djg
Structure name
adgrl3-lectin domain in complex with an activating synthetic antibody fragment
Structure deposition date
2022-06-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9HAR2
Residue number A
36
Residue number B
66
Peptide name
Adhesion G protein-coupled receptor L3
Ligandability
Cysteine 36 of Adhesion G protein-coupled receptor L3
Cysteine 66 of Adhesion G protein-coupled receptor L3
5ftu C 113 C 191
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor L3 between cysteines 113 and 191.
Details
Redox score ?
81
PDB code
5ftu
Structure name
tetrameric complex of latrophilin 3, unc5d and flrt2
Structure deposition date
2016-01-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
4
Peptide accession
Q80TS3
Residue number A
113
Residue number B
191
Peptide name
Adhesion G protein-coupled receptor L3
Ligandability
Cysteine 113 of Adhesion G protein-coupled receptor L3
Cysteine 191 of Adhesion G protein-coupled receptor L3
7sf7 A 882 A 904
A redox-regulated disulphide may form within Isoform 1 of Adhesion G protein-coupled receptor L3 between cysteines 882 and 904.
Details
Redox score ?
73
PDB code
7sf7
Structure name
lphn3 (adgrl3) 7tm domain bound to tethered agonist in complex with g protein heterotrimer
Structure deposition date
2021-10-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
8
% buried
84
Peptide accession
Q9HAR2-1
Residue number A
882
Residue number B
904
Peptide name
Isoform 1 of Adhesion G protein-coupled receptor L3
Ligandability
Cysteine 882 of Isoform 1 of Adhesion G protein-coupled receptor L3
Cysteine 904 of Isoform 1 of Adhesion G protein-coupled receptor L3
5ftu C 203 C 385
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor L3 between cysteines 203 and 385.
Details
Redox score ?
73
PDB code
5ftu
Structure name
tetrameric complex of latrophilin 3, unc5d and flrt2
Structure deposition date
2016-01-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
44
Peptide accession
Q80TS3
Residue number A
203
Residue number B
385
Peptide name
Adhesion G protein-coupled receptor L3
Ligandability
Cysteine 203 of Adhesion G protein-coupled receptor L3
Cysteine 385 of Adhesion G protein-coupled receptor L3
7x10 R 963 R 1192
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor L3 between cysteines 963 and 1192.
Details
Redox score ?
68
PDB code
7x10
Structure name
adgrl3/minig12 complex
Structure deposition date
2022-02-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
13
% buried
69
Peptide accession
Q80TS3
Residue number A
963
Residue number B
1192
Peptide name
Adhesion G protein-coupled receptor L3
Ligandability
Cysteine 963 of Adhesion G protein-coupled receptor L3
Cysteine 1192 of Adhesion G protein-coupled receptor L3
7wy8 R 959 R 963
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor L3 between cysteines 959 and 963. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
7wy8
Structure name
adgrl3/gs complex
Structure deposition date
2022-02-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
46
Peptide accession
Q80TS3
Residue number A
959
Residue number B
963
Peptide name
Adhesion G protein-coupled receptor L3
Ligandability
Cysteine 959 of Adhesion G protein-coupled receptor L3
Cysteine 963 of Adhesion G protein-coupled receptor L3
7wy8 R 985 R 1192
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor L3 between cysteines 985 and 1192. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
7wy8
Structure name
adgrl3/gs complex
Structure deposition date
2022-02-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
9
% buried
85
Peptide accession
Q80TS3
Residue number A
985
Residue number B
1192
Peptide name
Adhesion G protein-coupled receptor L3
Ligandability
Cysteine 985 of Adhesion G protein-coupled receptor L3
Cysteine 1192 of Adhesion G protein-coupled receptor L3
7wyb R 959 R 1192
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor L3 between cysteines 959 and 1192. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
7wyb
Structure name
adgrl3/gi complex
Structure deposition date
2022-02-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
42
Peptide accession
Q80TS3
Residue number A
959
Residue number B
1192
Peptide name
Adhesion G protein-coupled receptor L3
Ligandability
Cysteine 959 of Adhesion G protein-coupled receptor L3
Cysteine 1192 of Adhesion G protein-coupled receptor L3
7wyb R 963 R 968
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor L3 between cysteines 963 and 968. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
7wyb
Structure name
adgrl3/gi complex
Structure deposition date
2022-02-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
54
Peptide accession
Q80TS3
Residue number A
963
Residue number B
968
Peptide name
Adhesion G protein-coupled receptor L3
Ligandability
Cysteine 963 of Adhesion G protein-coupled receptor L3
Cysteine 968 of Adhesion G protein-coupled receptor L3
5afb A 113 A 165
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor L3 between cysteines 113 and 165. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
5afb
Structure name
crystal structure of the latrophilin3 lectin and olfactomedin domains
Structure deposition date
2015-01-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q80TS3
Residue number A
113
Residue number B
165
Peptide name
Adhesion G protein-coupled receptor L3
Ligandability
Cysteine 113 of Adhesion G protein-coupled receptor L3
Cysteine 165 of Adhesion G protein-coupled receptor L3
5ftu K 113 K 159
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor L3 between cysteines 113 and 159. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
5ftu
Structure name
tetrameric complex of latrophilin 3, unc5d and flrt2
Structure deposition date
2016-01-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
11
% buried
35
Peptide accession
Q80TS3
Residue number A
113
Residue number B
159
Peptide name
Adhesion G protein-coupled receptor L3
Ligandability
Cysteine 113 of Adhesion G protein-coupled receptor L3
Cysteine 159 of Adhesion G protein-coupled receptor L3
7x10 R 968 R 985
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor L3 between cysteines 968 and 985. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
7x10
Structure name
adgrl3/minig12 complex
Structure deposition date
2022-02-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
9
% buried
60
Peptide accession
Q80TS3
Residue number A
968
Residue number B
985
Peptide name
Adhesion G protein-coupled receptor L3
Ligandability
Cysteine 968 of Adhesion G protein-coupled receptor L3
Cysteine 985 of Adhesion G protein-coupled receptor L3
7x10 R 959 R 985
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor L3 between cysteines 959 and 985. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
7x10
Structure name
adgrl3/minig12 complex
Structure deposition date
2022-02-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
9
% buried
62
Peptide accession
Q80TS3
Residue number A
959
Residue number B
985
Peptide name
Adhesion G protein-coupled receptor L3
Ligandability
Cysteine 959 of Adhesion G protein-coupled receptor L3
Cysteine 985 of Adhesion G protein-coupled receptor L3
7wyb R 1152 R 1192
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor L3 between cysteines 1152 and 1192. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
7wyb
Structure name
adgrl3/gi complex
Structure deposition date
2022-02-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
12
% buried
74
Peptide accession
Q80TS3
Residue number A
1152
Residue number B
1192
Peptide name
Adhesion G protein-coupled receptor L3
Ligandability
Cysteine 1152 of Adhesion G protein-coupled receptor L3
Cysteine 1192 of Adhesion G protein-coupled receptor L3
7wy5 R 963 R 1152
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor L3 between cysteines 963 and 1152. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
7wy5
Structure name
adgrl3/gq complex
Structure deposition date
2022-02-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
68
Minimum pKa ?
12
% buried
80
Peptide accession
Q80TS3
Residue number A
963
Residue number B
1152
Peptide name
Adhesion G protein-coupled receptor L3
Ligandability
Cysteine 963 of Adhesion G protein-coupled receptor L3
Cysteine 1152 of Adhesion G protein-coupled receptor L3
7sf7 A 904 A 1062
A redox-regulated disulphide may form within Isoform 1 of Adhesion G protein-coupled receptor L3 between cysteines 904 and 1062. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
7sf7
Structure name
lphn3 (adgrl3) 7tm domain bound to tethered agonist in complex with g protein heterotrimer
Structure deposition date
2021-10-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
95
Peptide accession
Q9HAR2-1
Residue number A
904
Residue number B
1062
Peptide name
Isoform 1 of Adhesion G protein-coupled receptor L3
Ligandability
Cysteine 904 of Isoform 1 of Adhesion G protein-coupled receptor L3
Cysteine 1062 of Isoform 1 of Adhesion G protein-coupled receptor L3
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