ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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C-X-C chemokine receptor type 1

Intramolecular
Cysteine 30 and cysteine 277
Cysteine 110 and cysteine 187
Cysteine 157 and cysteine 160
Cysteine 130 and cysteine 157
Cysteine 130 and cysteine 160
Cysteine 254 and cysteine 299
A redox-regulated disulphide may form within C-X-C chemokine receptor type 1 between cysteines 30 and 277.

Details

Redox score ?
84
PDB code
2lnl
Structure name
structure of human cxcr1 in phospholipid bilayers
Structure deposition date
2011-12-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P25024
Residue number A
30
Residue number B
277
Peptide name
C-X-C chemokine receptor type 1

Ligandability

Cysteine 30 of C-X-C chemokine receptor type 1

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 277 of C-X-C chemokine receptor type 1

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 1 between cysteines 110 and 187.

Details

Redox score ?
82
PDB code
2lnl
Structure name
structure of human cxcr1 in phospholipid bilayers
Structure deposition date
2011-12-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P25024
Residue number A
110
Residue number B
187
Peptide name
C-X-C chemokine receptor type 1

Ligandability

Cysteine 110 of C-X-C chemokine receptor type 1

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 187 of C-X-C chemokine receptor type 1

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 1 between cysteines 157 and 160.

Details

Redox score ?
61
PDB code
2lnl
Structure name
structure of human cxcr1 in phospholipid bilayers
Structure deposition date
2011-12-31
Thiol separation (Å)
6
Half-sphere exposure sum ?
56
Minimum pKa ?
9
% buried
42
Peptide accession
P25024
Residue number A
157
Residue number B
160
Peptide name
C-X-C chemokine receptor type 1

Ligandability

Cysteine 157 of C-X-C chemokine receptor type 1

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 160 of C-X-C chemokine receptor type 1

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 1 between cysteines 130 and 157. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
2lnl
Structure name
structure of human cxcr1 in phospholipid bilayers
Structure deposition date
2011-12-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
9
% buried
62
Peptide accession
P25024
Residue number A
130
Residue number B
157
Peptide name
C-X-C chemokine receptor type 1

Ligandability

Cysteine 130 of C-X-C chemokine receptor type 1

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 157 of C-X-C chemokine receptor type 1

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 1 between cysteines 130 and 160. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
2lnl
Structure name
structure of human cxcr1 in phospholipid bilayers
Structure deposition date
2011-12-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
54
Peptide accession
P25024
Residue number A
130
Residue number B
160
Peptide name
C-X-C chemokine receptor type 1

Ligandability

Cysteine 130 of C-X-C chemokine receptor type 1

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 160 of C-X-C chemokine receptor type 1

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 1 between cysteines 254 and 299. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
2lnl
Structure name
structure of human cxcr1 in phospholipid bilayers
Structure deposition date
2011-12-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
42
Minimum pKa ?
9
% buried
18
Peptide accession
P25024
Residue number A
254
Residue number B
299
Peptide name
C-X-C chemokine receptor type 1

Ligandability

Cysteine 254 of C-X-C chemokine receptor type 1

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 299 of C-X-C chemokine receptor type 1

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.

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