ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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C-X-C chemokine receptor type 2

Intramolecular
Cysteine 39 and cysteine 286
Cysteine 119 and cysteine 196
Cysteine 139 and cysteine 166
Cysteine 263 and cysteine 308
Cysteine 139 and cysteine 230
Cysteine 263 and cysteine 166
Cysteine 1004 and cysteine 166
A redox-regulated disulphide may form within C-X-C chemokine receptor type 2 between cysteines 39 and 286.

Details

Redox score ?
86
PDB code
6lfm
Structure name
cryo-em structure of a class a gpcr
Structure deposition date
2019-12-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P25025
Residue number A
39
Residue number B
286
Peptide name
C-X-C chemokine receptor type 2

Ligandability

Cysteine 39 of C-X-C chemokine receptor type 2

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 286 of C-X-C chemokine receptor type 2

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 C-X-C chemokine receptor type 2 between cysteines 119 and 196.

Details

Redox score ?
85
PDB code
6lfl
Structure name
crystal structure of a class a gpcr
Structure deposition date
2019-12-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P25025
Residue number A
119
Residue number B
196
Peptide name
C-X-C chemokine receptor type 2

Ligandability

Cysteine 119 of C-X-C chemokine receptor type 2

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 196 of C-X-C chemokine receptor type 2

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 C-X-C chemokine receptor type 2 between cysteines 139 and 166. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
6lfl
Structure name
crystal structure of a class a gpcr
Structure deposition date
2019-12-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
62
Peptide accession
P25025
Residue number A
139
Residue number B
166
Peptide name
C-X-C chemokine receptor type 2

Ligandability

Cysteine 139 of C-X-C chemokine receptor type 2

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 166 of C-X-C chemokine receptor type 2

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 C-X-C chemokine receptor type 2 between cysteines 263 and 308. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
6lfl
Structure name
crystal structure of a class a gpcr
Structure deposition date
2019-12-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
52
Peptide accession
P25025
Residue number A
263
Residue number B
308
Peptide name
C-X-C chemokine receptor type 2

Ligandability

Cysteine 263 of C-X-C chemokine receptor type 2

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 308 of C-X-C chemokine receptor type 2

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 C-X-C chemokine receptor type 2 between cysteines 139 and 230. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
6lfm
Structure name
cryo-em structure of a class a gpcr
Structure deposition date
2019-12-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
78
Peptide accession
P25025
Residue number A
139
Residue number B
230
Peptide name
C-X-C chemokine receptor type 2

Ligandability

Cysteine 139 of C-X-C chemokine receptor type 2

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 230 of C-X-C chemokine receptor type 2

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 C-X-C chemokine receptor type 2 between cysteines 263 and 166 (15 and 16 respectively in this structure).

Details

Redox score ?
nan
PDB code
4mpa
Structure name
crystal structure of nherf1-cxcr2 signaling complex in p21 space group
Structure deposition date
2013-09-12
Thiol separation (Å)
7
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
19
Peptide accession
P25025
Residue number A
263
Residue number B
166
Peptide name
C-X-C chemokine receptor type 2

Ligandability

Cysteine 263 of C-X-C chemokine receptor type 2

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 166 of C-X-C chemokine receptor type 2

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.

Uncertain whether structure cysteine 15 has been assigned to correct residue.
Uncertain whether structure cysteine 16 has been assigned to correct residue.
A redox-regulated disulphide may form within C-X-C chemokine receptor type 2 between cysteines 1004 and 166 (1004 and 1133 respectively in this structure).

Details

Redox score ?
nan
PDB code
6lfl
Structure name
crystal structure of a class a gpcr
Structure deposition date
2019-12-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
9
% buried
42
Peptide accession
P25025
Residue number A
1004
Residue number B
166
Peptide name
C-X-C chemokine receptor type 2

Ligandability

Cysteine 1004 of C-X-C chemokine receptor type 2

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 166 of C-X-C chemokine receptor type 2

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 1004 in protein A could not be asigned to a Uniprot residue.
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