ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Apelin receptor

Intramolecular
Cysteine 19 and cysteine 281
Cysteine 102 and cysteine 181
Cysteine 260 and cysteine 220
Cysteine 260 and cysteine 320
Cysteine 260 and cysteine 296
Cysteine 220 and cysteine 320
Cysteine 260 and cysteine 303
Cysteine 294 and cysteine 296
Cysteine 296 and cysteine 303
Cysteine 1009 and cysteine 1042
More...
Cysteine 1039 and cysteine 1042
Cysteine 1006 and cysteine 1039
A redox-regulated disulphide may form within Apelin receptor between cysteines 19 and 281.

Details

Redox score ?
85
PDB code
6knm
Structure name
apelin receptor in complex with single domain antibody
Structure deposition date
2019-08-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35414
Residue number A
19
Residue number B
281
Peptide name
Apelin receptor

Ligandability

Cysteine 19 of Apelin receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 281 of Apelin receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Apelin receptor between cysteines 102 and 181.

Details

Redox score ?
84
PDB code
5vbl
Structure name
structure of apelin receptor in complex with agonist peptide
Structure deposition date
2017-03-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35414
Residue number A
102
Residue number B
181
Peptide name
Apelin receptor

Ligandability

Cysteine 102 of Apelin receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 181 of Apelin receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Apelin receptor between cysteines 260 and 220 (217 and 220 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
7sus
Structure name
crystal structure of apelin receptor in complex with small molecule
Structure deposition date
2021-11-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
60
Peptide accession
P35414
Residue number A
260
Residue number B
220
Peptide name
Apelin receptor

Ligandability

Cysteine 260 of Apelin receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 220 of Apelin receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Apelin receptor between cysteines 260 and 320 (217 and 250 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
7sus
Structure name
crystal structure of apelin receptor in complex with small molecule
Structure deposition date
2021-11-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
77
Peptide accession
P35414
Residue number A
260
Residue number B
320
Peptide name
Apelin receptor

Ligandability

Cysteine 260 of Apelin receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 320 of Apelin receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Apelin receptor between cysteines 260 and 296. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
7w0m
Structure name
cryo-em structure of a monomeric gpcr-gi complex with small molecule
Structure deposition date
2021-11-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
36
Peptide accession
P35414
Residue number A
260
Residue number B
296
Peptide name
Apelin receptor

Ligandability

Cysteine 260 of Apelin receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 296 of Apelin receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Apelin receptor between cysteines 220 and 320 (220 and 250 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
7sus
Structure name
crystal structure of apelin receptor in complex with small molecule
Structure deposition date
2021-11-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
66
Peptide accession
P35414
Residue number A
220
Residue number B
320
Peptide name
Apelin receptor

Ligandability

Cysteine 220 of Apelin receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 320 of Apelin receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Apelin receptor between cysteines 260 and 303. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
6knm
Structure name
apelin receptor in complex with single domain antibody
Structure deposition date
2019-08-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
10
% buried
59
Peptide accession
P35414
Residue number A
260
Residue number B
303
Peptide name
Apelin receptor

Ligandability

Cysteine 260 of Apelin receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 303 of Apelin receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Apelin receptor between cysteines 294 and 296. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7sus
Structure name
crystal structure of apelin receptor in complex with small molecule
Structure deposition date
2021-11-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
40
Peptide accession
P35414
Residue number A
294
Residue number B
296
Peptide name
Apelin receptor

Ligandability

Cysteine 294 of Apelin receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 296 of Apelin receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Apelin receptor between cysteines 296 and 303. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
7sus
Structure name
crystal structure of apelin receptor in complex with small molecule
Structure deposition date
2021-11-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
10
% buried
46
Peptide accession
P35414
Residue number A
296
Residue number B
303
Peptide name
Apelin receptor

Ligandability

Cysteine 296 of Apelin receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 303 of Apelin receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Apelin receptor between cysteines 1009 and 1042.

Details

Redox score ?
nan
PDB code
6knm
Structure name
apelin receptor in complex with single domain antibody
Structure deposition date
2019-08-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
9
% buried
0
Peptide accession
P35414
Residue number A
1009
Residue number B
1042
Peptide name
Apelin receptor

Ligandability

Cysteine 1009 of Apelin receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1042 of Apelin receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1009 in protein A could not be asigned to a Uniprot residue.
Cysteine 1042 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Apelin receptor between cysteines 1039 and 1042.

Details

Redox score ?
nan
PDB code
5vbl
Structure name
structure of apelin receptor in complex with agonist peptide
Structure deposition date
2017-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
8
% buried
4
Peptide accession
P35414
Residue number A
1039
Residue number B
1042
Peptide name
Apelin receptor

Ligandability

Cysteine 1039 of Apelin receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1042 of Apelin receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1039 in protein A could not be asigned to a Uniprot residue.
Cysteine 1042 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Apelin receptor between cysteines 1006 and 1039.

Details

Redox score ?
nan
PDB code
6knm
Structure name
apelin receptor in complex with single domain antibody
Structure deposition date
2019-08-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
5
% buried
5
Peptide accession
P35414
Residue number A
1006
Residue number B
1039
Peptide name
Apelin receptor

Ligandability

Cysteine 1006 of Apelin receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1039 of Apelin receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1006 in protein A could not be asigned to a Uniprot residue.
Cysteine 1039 in protein B could not be asigned to a Uniprot residue.
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