Interleukin-25

Peptide B accession

Peptide A residue number

170

Peptide B residue number

170

Ligandability

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Interleukin-25 at cysteines 115 and 170. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

structure of the higher-order il-25-il-17rb complex

Structure deposition date

2022-05-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Interleukin-25

Peptide B name

Interleukin-25

Peptide A accession

Peptide B accession

Peptide A residue number

115

Peptide B residue number

170

Ligandability

Cysteine 115 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

Cysteine 170 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Interleukin-25 at cysteines 115 and 115. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

structure of the homodimeric il-25-il-17rb binary complex

Structure deposition date

2022-05-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Interleukin-25

Peptide B name

Interleukin-25

Peptide A accession

Peptide B accession

Peptide A residue number

115

Peptide B residue number

115

Ligandability

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Interleukin-25 between cysteines 74 and 112.

Details

Redox score ?

PDB code

Structure name

structure of the homodimeric il-25-il-17rb binary complex

Structure deposition date

2022-05-03

Thiol separation (Å)

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

Residue number B

112

Peptide name

Interleukin-25

Ligandability

Cysteine 74 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

Cysteine 112 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Interleukin-25 between cysteines 110 and 168.

Details

Redox score ?

PDB code

Structure name

structure of the homodimeric il-25-il-17rb binary complex

Structure deposition date

2022-05-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

110

Residue number B

168

Peptide name

Interleukin-25

Ligandability

Cysteine 110 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

Cysteine 168 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Interleukin-25 between cysteines 110 and 112. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

structure of the higher-order il-25-il-17rb complex

Structure deposition date

2022-05-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

nan

Peptide accession

Residue number A

110

Residue number B

112

Peptide name

Interleukin-25

Ligandability

Cysteine 110 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

Cysteine 112 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Interleukin-25 between cysteines 145 and 156. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

structure of the higher-order il-25-il-17rb complex

Structure deposition date

2022-05-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

145

Residue number B

156

Peptide name

Interleukin-25

Ligandability

Cysteine 145 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

Cysteine 156 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Interleukin-25 between cysteines 74 and 115. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

structure of the homodimeric il-25-il-17rb binary complex

Structure deposition date

2022-05-03

Thiol separation (Å)

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

Residue number B

115

Peptide name

Interleukin-25

Ligandability

Cysteine 74 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

Cysteine 115 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Interleukin-25 between cysteines 112 and 115. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

structure of the homodimeric il-25-il-17rb binary complex

Structure deposition date

2022-05-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

112

Residue number B

115

Peptide name

Interleukin-25

Ligandability

Cysteine 112 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

Cysteine 115 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Interleukin-25 between cysteines 110 and 115. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

structure of the higher-order il-25-il-17rb complex

Structure deposition date

2022-05-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

110

Residue number B

115

Peptide name

Interleukin-25

Ligandability

Cysteine 110 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

Cysteine 115 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Interleukin-25 between cysteines 74 and 110. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

structure of the homodimeric il-25-il-17rb binary complex

Structure deposition date

2022-05-03

Thiol separation (Å)

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

Residue number B

110

Peptide name

Interleukin-25

Ligandability

Cysteine 74 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

Cysteine 110 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Interleukin-25 between cysteines 112 and 168. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

structure of the higher-order il-25-il-17rb complex

Structure deposition date

2022-05-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

nan

Peptide accession

Residue number A

112

Residue number B

168

Peptide name

Interleukin-25

Ligandability

Cysteine 112 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

Cysteine 168 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Interleukin-25 between cysteines 74 and 168. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

structure of the homodimeric il-25-il-17rb binary complex

Structure deposition date

2022-05-03

Thiol separation (Å)

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

Residue number B

168

Peptide name

Interleukin-25

Ligandability

Cysteine 74 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

Cysteine 168 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Interleukin-25 between cysteines 110 and 170. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

structure of the higher-order il-25-il-17rb complex

Structure deposition date

2022-05-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

110

Residue number B

170

Peptide name

Interleukin-25

Ligandability

Cysteine 110 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

Cysteine 170 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Interleukin-25 between cysteines 115 and 168. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

structure of the higher-order il-25-il-17rb complex

Structure deposition date

2022-05-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

115

Residue number B

168

Peptide name

Interleukin-25

Ligandability

Cysteine 115 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

Cysteine 168 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Interleukin-25 between cysteines 168 and 170. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

structure of the higher-order il-25-il-17rb complex

Structure deposition date

2022-05-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

168

Residue number B

170

Peptide name

Interleukin-25

Ligandability

Cysteine 168 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.

Cysteine 170 of Interleukin-25

Not ligandable in the dataset of Vinogradova et al.