a tool for identifying drug-targetable redox-active disulphides

LIR-1

Intramolecular

Cysteine 157 and cysteine 167

Cysteine 49 and cysteine 98

Cysteine 145 and cysteine 197

Cysteine 157 and cysteine 197

Cysteine 145 and cysteine 157

A redox-regulated disulphide may form within LIR-1 between cysteines 157 and 167 (134 and 144 respectively in this structure).

Details

Redox score ?

85

PDB code

Structure name

crystal structure of hla-a2 in complex with lilrb1

Structure deposition date

2017-11-03

Thiol separation (Å)

2

Half-sphere exposure sum ?

47

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

157

Residue number B

167

Peptide name

LIR-1

Ligandability

Cysteine 157 of LIR-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 167 of LIR-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 LIR-1 between cysteines 49 and 98 (26 and 75 respectively in this structure).

Details

Redox score ?

83

PDB code

Structure name

crystal structure of hla-a2 in complex with lilrb1

Structure deposition date

2017-11-03

Thiol separation (Å)

2

Half-sphere exposure sum ?

75

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

49

Residue number B

98

Peptide name

LIR-1

Ligandability

Cysteine 49 of LIR-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 98 of LIR-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 LIR-1 between cysteines 145 and 197 (122 and 174 respectively in this structure).

Details

Redox score ?

79

PDB code

Structure name

crystal structure of hla-a2 in complex with lilrb1

Structure deposition date

2017-11-03

Thiol separation (Å)

2

Half-sphere exposure sum ?

89

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

145

Residue number B

197

Peptide name

LIR-1

Ligandability

Cysteine 145 of LIR-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 197 of LIR-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 LIR-1 between cysteines 157 and 197 (134 and 174 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

Structure name

crystal structure of hla-a2 in complex with lilrb1

Structure deposition date

2017-11-03

Thiol separation (Å)

9

Half-sphere exposure sum ?

73

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

157

Residue number B

197

Peptide name

LIR-1

Ligandability

Cysteine 157 of LIR-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 197 of LIR-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 LIR-1 between cysteines 145 and 157 (122 and 134 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

36

PDB code

Structure name

crystal structure of hla-a2 in complex with lilrb1

Structure deposition date

2017-11-03

Thiol separation (Å)

10

Half-sphere exposure sum ?

73

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

145

Residue number B

157

Peptide name

LIR-1

Ligandability

Cysteine 145 of LIR-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 LIR-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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