a tool for identifying drug-targetable redox-active disulphides

Interleukin-12 subunit alpha

Intermolecular

Cysteine 199 of Interleukin-12 subunit beta and cysteine 96

Intramolecular

Cysteine 64 and cysteine 196

Cysteine 37 and cysteine 110

Cysteine 85 and cysteine 123

A redox-regulated disulphide may form between cysteine 199 of Interleukin-12 subunit beta and cysteine 96 of Interleukin-12 subunit alpha (177 and 74 respectively in this structure).

Details

Redox score ?

88

PDB code

Structure name

human interleukin-12

Structure deposition date

2000-06-07

Thiol separation (Å)

2

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Interleukin-12 subunit beta

Peptide B name

Interleukin-12 subunit alpha

Peptide A accession

Peptide B accession

Peptide A residue number

199

Peptide B residue number

96

Ligandability

Cysteine 199 of Interleukin-12 subunit beta

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 96 of Interleukin-12 subunit alpha

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 Interleukin-12 subunit alpha between cysteines 64 and 196 (42 and 174 respectively in this structure).

Details

Redox score ?

88

PDB code

Structure name

human interleukin-12

Structure deposition date

2000-06-07

Thiol separation (Å)

2

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

64

Residue number B

196

Peptide name

Interleukin-12 subunit alpha

Ligandability

Cysteine 64 of Interleukin-12 subunit alpha

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 Interleukin-12 subunit alpha

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 Interleukin-12 subunit alpha between cysteines 37 and 110 (15 and 88 respectively in this structure).

Details

Redox score ?

85

PDB code

Structure name

crystal structure of ustekinumab fab/il-12 complex

Structure deposition date

2009-05-29

Thiol separation (Å)

2

Half-sphere exposure sum ?

67

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

37

Residue number B

110

Peptide name

Interleukin-12 subunit alpha

Ligandability

Cysteine 37 of Interleukin-12 subunit alpha

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 110 of Interleukin-12 subunit alpha

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 Interleukin-12 subunit alpha between cysteines 85 and 123 (63 and 101 respectively in this structure).

Details

Redox score ?

81

PDB code

Structure name

crystal structure of ustekinumab fab/il-12 complex

Structure deposition date

2009-05-29

Thiol separation (Å)

2

Half-sphere exposure sum ?

77

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

85

Residue number B

123

Peptide name

Interleukin-12 subunit alpha

Ligandability

Cysteine 85 of Interleukin-12 subunit alpha

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 123 of Interleukin-12 subunit alpha

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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