Calcitonin gene-related peptide type 1 receptor
Intermolecular
Cysteine 115 of Pro-adrenomedullin and cysteine 299
Cysteine 110 of Pro-adrenomedullin and cysteine 299
Cysteine 89 of Calcitonin gene-related peptide 1 and cysteine 299
Cysteine 84 of Calcitonin gene-related peptide 1 and cysteine 299
Cysteine 110 of Protein ADM2 and cysteine 299
Intramolecular
Cysteine 88 and cysteine 127
Cysteine 299 and cysteine 171
Cysteine 212 and cysteine 282
Cysteine 65 and cysteine 105
Cysteine 48 and cysteine 74
More...Cysteine 186 and cysteine 225
Cysteine 225 and cysteine 232
Cysteine 105 and cysteine 436
Cysteine 186 and cysteine 74
Cysteine 105 and cysteine 282
Cysteine 74 and cysteine 225
Cysteine 105 and cysteine 1104
Cysteine 48 and cysteine 1099
6uun P 21 R 299
A redox-regulated disulphide may form between cysteine 115 of Pro-adrenomedullin and cysteine 299 of Calcitonin gene-related peptide type 1 receptor (21 and 299 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
6uun
Structure name
cryoem structure of the active adrenomedullin 1 receptor g protein complex with adrenomedullin peptide
Structure deposition date
2019-10-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
nan
Peptide A name
Pro-adrenomedullin
Peptide B name
Calcitonin gene-related peptide type 1 receptor
Peptide A accession
P35318
Peptide B accession
Q16602
Peptide A residue number
115
Peptide B residue number
299
Ligandability
Cysteine 115 of Pro-adrenomedullin
Cysteine 299 of Calcitonin gene-related peptide type 1 receptor
6uun P 16 R 299
A redox-regulated disulphide may form between cysteine 110 of Pro-adrenomedullin and cysteine 299 of Calcitonin gene-related peptide type 1 receptor (16 and 299 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
6uun
Structure name
cryoem structure of the active adrenomedullin 1 receptor g protein complex with adrenomedullin peptide
Structure deposition date
2019-10-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
11
% buried
nan
Peptide A name
Pro-adrenomedullin
Peptide B name
Calcitonin gene-related peptide type 1 receptor
Peptide A accession
P35318
Peptide B accession
Q16602
Peptide A residue number
110
Peptide B residue number
299
Ligandability
Cysteine 110 of Pro-adrenomedullin
Cysteine 299 of Calcitonin gene-related peptide type 1 receptor
6e3y P 7 R 299
A redox-regulated disulphide may form between cysteine 89 of Calcitonin gene-related peptide 1 and cysteine 299 of Calcitonin gene-related peptide type 1 receptor (7 and 299 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
6e3y
Structure name
cryo-em structure of the active, gs-protein complexed, human cgrp receptor
Structure deposition date
2018-07-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
77
Minimum pKa ?
11
% buried
nan
Peptide A name
Calcitonin gene-related peptide 1
Peptide B name
Calcitonin gene-related peptide type 1 receptor
Peptide A accession
P06881
Peptide B accession
Q16602
Peptide A residue number
89
Peptide B residue number
299
Ligandability
Cysteine 89 of Calcitonin gene-related peptide 1
Cysteine 299 of Calcitonin gene-related peptide type 1 receptor
6e3y P 2 R 299
A redox-regulated disulphide may form between cysteine 84 of Calcitonin gene-related peptide 1 and cysteine 299 of Calcitonin gene-related peptide type 1 receptor (2 and 299 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
6e3y
Structure name
cryo-em structure of the active, gs-protein complexed, human cgrp receptor
Structure deposition date
2018-07-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
63
Minimum pKa ?
11
% buried
nan
Peptide A name
Calcitonin gene-related peptide 1
Peptide B name
Calcitonin gene-related peptide type 1 receptor
Peptide A accession
P06881
Peptide B accession
Q16602
Peptide A residue number
84
Peptide B residue number
299
Ligandability
Cysteine 84 of Calcitonin gene-related peptide 1
Cysteine 299 of Calcitonin gene-related peptide type 1 receptor
6uva P 10 R 299
A redox-regulated disulphide may form between cysteine 110 of Protein ADM2 and cysteine 299 of Calcitonin gene-related peptide type 1 receptor (10 and 299 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
6uva
Structure name
cryoem structure of the active adrenomedullin 2 receptor g protein complex with adrenomedullin 2 peptide
Structure deposition date
2019-11-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
nan
Peptide A name
Protein ADM2
Peptide B name
Calcitonin gene-related peptide type 1 receptor
Peptide A accession
Q7Z4H4
Peptide B accession
Q16602
Peptide A residue number
110
Peptide B residue number
299
Ligandability
Cysteine 110 of Protein ADM2
Cysteine 299 of Calcitonin gene-related peptide type 1 receptor
8ax7 A 2088 A 2127
A redox-regulated disulphide may form within Calcitonin gene-related peptide type 1 receptor between cysteines 88 and 127 (2088 and 2127 respectively in this structure).
Details
Redox score ?
87
PDB code
8ax7
Structure name
crystal structure of a cgrp receptor ectodomain heterodimer bound to macrocyclic inhibitor htl0031448
Structure deposition date
2022-08-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16602
Residue number A
88
Residue number B
127
Peptide name
Calcitonin gene-related peptide type 1 receptor
Ligandability
Cysteine 88 of Calcitonin gene-related peptide type 1 receptor
Cysteine 127 of Calcitonin gene-related peptide type 1 receptor
6v2e A 1084 A 1131
A redox-regulated disulphide may form within Calcitonin gene-related peptide type 1 receptor between cysteines 299 and 171 (1084 and 1131 respectively in this structure).
Details
Redox score ?
87
PDB code
6v2e
Structure name
crystal structure of the human clr:ramp2 extracellular domain heterodimer with bound high-affinity adrenomedullin s45r/k46l/s48g/q50w variant
Structure deposition date
2019-11-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16602
Residue number A
299
Residue number B
171
Peptide name
Calcitonin gene-related peptide type 1 receptor
Ligandability
Cysteine 299 of Calcitonin gene-related peptide type 1 receptor
Cysteine 171 of Calcitonin gene-related peptide type 1 receptor
6uva R 212 R 282
A redox-regulated disulphide may form within Calcitonin gene-related peptide type 1 receptor between cysteines 212 and 282.
Details
Redox score ?
85
PDB code
6uva
Structure name
cryoem structure of the active adrenomedullin 2 receptor g protein complex with adrenomedullin 2 peptide
Structure deposition date
2019-11-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16602
Residue number A
212
Residue number B
282
Peptide name
Calcitonin gene-related peptide type 1 receptor
Ligandability
Cysteine 212 of Calcitonin gene-related peptide type 1 receptor
Cysteine 282 of Calcitonin gene-related peptide type 1 receptor
3n7p B 65 B 105
A redox-regulated disulphide may form within Calcitonin gene-related peptide type 1 receptor between cysteines 65 and 105.
Details
Redox score ?
85
PDB code
3n7p
Structure name
crystal structure of the ectodomain complex of the cgrp receptor, a class-b gpcr, reveals the site of drug antagonism
Structure deposition date
2010-05-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16602
Residue number A
65
Residue number B
105
Peptide name
Calcitonin gene-related peptide type 1 receptor
Ligandability
Cysteine 65 of Calcitonin gene-related peptide type 1 receptor
Cysteine 105 of Calcitonin gene-related peptide type 1 receptor
5v6y D 2048 D 2074
A redox-regulated disulphide may form within Calcitonin gene-related peptide type 1 receptor between cysteines 48 and 74 (2048 and 2074 respectively in this structure).
Details
Redox score ?
80
PDB code
5v6y
Structure name
crystal structure of the human clr:ramp1 extracellular domain heterodimer with bound high-affinity and altered selectivity adrenomedullin variant
Structure deposition date
2017-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16602
Residue number A
48
Residue number B
74
Peptide name
Calcitonin gene-related peptide type 1 receptor
Ligandability
Cysteine 48 of Calcitonin gene-related peptide type 1 receptor
Cysteine 74 of Calcitonin gene-related peptide type 1 receptor
6e3y R 186 R 225
A redox-regulated disulphide may form within Calcitonin gene-related peptide type 1 receptor between cysteines 186 and 225. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
6e3y
Structure name
cryo-em structure of the active, gs-protein complexed, human cgrp receptor
Structure deposition date
2018-07-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
10
% buried
66
Peptide accession
Q16602
Residue number A
186
Residue number B
225
Peptide name
Calcitonin gene-related peptide type 1 receptor
Ligandability
Cysteine 186 of Calcitonin gene-related peptide type 1 receptor
Cysteine 225 of Calcitonin gene-related peptide type 1 receptor
7knt R 225 R 232
A redox-regulated disulphide may form within Calcitonin gene-related peptide type 1 receptor between cysteines 225 and 232. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
26
PDB code
7knt
Structure name
cryoem structure of the apo-cgrp receptor in a detergent micelle
Structure deposition date
2020-11-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
93
Peptide accession
Q16602
Residue number A
225
Residue number B
232
Peptide name
Calcitonin gene-related peptide type 1 receptor
Ligandability
Cysteine 225 of Calcitonin gene-related peptide type 1 receptor
Cysteine 232 of Calcitonin gene-related peptide type 1 receptor
5v6y B 1057 B 1104
A redox-regulated disulphide may form within Calcitonin gene-related peptide type 1 receptor between cysteines 105 and 436 (1057 and 1104 respectively in this structure).
Details
Redox score ?
nan
PDB code
5v6y
Structure name
crystal structure of the human clr:ramp1 extracellular domain heterodimer with bound high-affinity and altered selectivity adrenomedullin variant
Structure deposition date
2017-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16602
Residue number A
105
Residue number B
436
Peptide name
Calcitonin gene-related peptide type 1 receptor
Ligandability
Cysteine 105 of Calcitonin gene-related peptide type 1 receptor
Cysteine 436 of Calcitonin gene-related peptide type 1 receptor
Uncertain whether structure cysteine 1057 has been assigned to correct residue.
Uncertain whether structure cysteine 1104 has been assigned to correct residue.
7p0i A 1027 A 1082
A redox-regulated disulphide may form within Calcitonin gene-related peptide type 1 receptor between cysteines 186 and 74 (1027 and 1082 respectively in this structure).
Details
Redox score ?
nan
PDB code
7p0i
Structure name
crystal structure of a cgrp receptor ectodomain heterodimer bound to macrocyclic inhibitor compound 13
Structure deposition date
2021-06-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16602
Residue number A
186
Residue number B
74
Peptide name
Calcitonin gene-related peptide type 1 receptor
Ligandability
Cysteine 186 of Calcitonin gene-related peptide type 1 receptor
Cysteine 74 of Calcitonin gene-related peptide type 1 receptor
Uncertain whether structure cysteine 1027 has been assigned to correct residue.
Uncertain whether structure cysteine 1082 has been assigned to correct residue.
5v6y D 1057 D 1104
A redox-regulated disulphide may form within Calcitonin gene-related peptide type 1 receptor between cysteines 105 and 282 (1057 and 1104 respectively in this structure).
Details
Redox score ?
nan
PDB code
5v6y
Structure name
crystal structure of the human clr:ramp1 extracellular domain heterodimer with bound high-affinity and altered selectivity adrenomedullin variant
Structure deposition date
2017-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16602
Residue number A
105
Residue number B
282
Peptide name
Calcitonin gene-related peptide type 1 receptor
Ligandability
Cysteine 105 of Calcitonin gene-related peptide type 1 receptor
Cysteine 282 of Calcitonin gene-related peptide type 1 receptor
Uncertain whether structure cysteine 1057 has been assigned to correct residue.
Uncertain whether structure cysteine 1104 has been assigned to correct residue.
6d1u C 1040 C 1072
A redox-regulated disulphide may form within Calcitonin gene-related peptide type 1 receptor between cysteines 74 and 225 (1040 and 1072 respectively in this structure).
Details
Redox score ?
nan
PDB code
6d1u
Structure name
crystal structure of the human clr:ramp1 extracellular domain heterodimer in complex with adrenomedullin 2/intermedin
Structure deposition date
2018-04-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16602
Residue number A
74
Residue number B
225
Peptide name
Calcitonin gene-related peptide type 1 receptor
Ligandability
Cysteine 74 of Calcitonin gene-related peptide type 1 receptor
Cysteine 225 of Calcitonin gene-related peptide type 1 receptor
Uncertain whether structure cysteine 1040 has been assigned to correct residue.
Uncertain whether structure cysteine 1072 has been assigned to correct residue.
7p0i A 1057 A 1104
A redox-regulated disulphide may form within Calcitonin gene-related peptide type 1 receptor between cysteines 105 and 1104 (1057 and 1104 respectively in this structure).
Details
Redox score ?
nan
PDB code
7p0i
Structure name
crystal structure of a cgrp receptor ectodomain heterodimer bound to macrocyclic inhibitor compound 13
Structure deposition date
2021-06-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16602
Residue number A
105
Residue number B
1104
Peptide name
Calcitonin gene-related peptide type 1 receptor
Ligandability
Cysteine 105 of Calcitonin gene-related peptide type 1 receptor
Cysteine 1104 of Calcitonin gene-related peptide type 1 receptor
Uncertain whether structure cysteine 1057 has been assigned to correct residue.
Cysteine 1104 in protein B could not be asigned to a Uniprot residue.
6v2e A 1068 A 1099
A redox-regulated disulphide may form within Calcitonin gene-related peptide type 1 receptor between cysteines 48 and 1099 (1068 and 1099 respectively in this structure).
Details
Redox score ?
nan
PDB code
6v2e
Structure name
crystal structure of the human clr:ramp2 extracellular domain heterodimer with bound high-affinity adrenomedullin s45r/k46l/s48g/q50w variant
Structure deposition date
2019-11-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16602
Residue number A
48
Residue number B
1099
Peptide name
Calcitonin gene-related peptide type 1 receptor
Ligandability
Cysteine 48 of Calcitonin gene-related peptide type 1 receptor
Cysteine 1099 of Calcitonin gene-related peptide type 1 receptor
Uncertain whether structure cysteine 1068 has been assigned to correct residue.
Cysteine 1099 in protein B could not be asigned to a Uniprot residue.
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