ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Interleukin-23 subunit alpha

Intermolecular
Cysteine 73 and cysteine 199 of Interleukin-12 subunit beta
Cysteine 77 and cysteine 199 of Interleukin-12 subunit beta
Intramolecular
Cysteine 77 and cysteine 89
Cysteine 73 and cysteine 77
A redox-regulated disulphide may form between cysteine 73 of Interleukin-23 subunit alpha and cysteine 199 of Interleukin-12 subunit beta (54 and 177 respectively in this structure).

Details

Redox score ?
82
PDB code
4grw
Structure name
structure of a complex of human il-23 with 3 nanobodies (llama vhhs)
Structure deposition date
2012-08-27
Thiol separation (Å)
3
Half-sphere exposure sum ?
48
Minimum pKa ?
8
% buried
36
Peptide A name
Interleukin-23 subunit alpha
Peptide B name
Interleukin-12 subunit beta
Peptide A accession
Q9NPF7
Peptide B accession
P29460
Peptide A residue number
73
Peptide B residue number
199

Ligandability

Cysteine 73 of Interleukin-23 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 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.

A redox-regulated disulphide may form between cysteine 77 of Interleukin-23 subunit alpha and cysteine 199 of Interleukin-12 subunit beta (58 and 177 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
3d85
Structure name
crystal structure of il-23 in complex with neutralizing fab
Structure deposition date
2008-05-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
nan
Peptide A name
Interleukin-23 subunit alpha
Peptide B name
Interleukin-12 subunit beta
Peptide A accession
Q9NPF7
Peptide B accession
P29460
Peptide A residue number
77
Peptide B residue number
199

Ligandability

Cysteine 77 of Interleukin-23 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 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.

A redox-regulated disulphide may form within Interleukin-23 subunit alpha between cysteines 77 and 89 (58 and 70 respectively in this structure).

Details

Redox score ?
73
PDB code
3d87
Structure name
crystal structure of interleukin-23
Structure deposition date
2008-05-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
81
Minimum pKa ?
9
% buried
96
Peptide accession
Q9NPF7
Residue number A
77
Residue number B
89
Peptide name
Interleukin-23 subunit alpha

Ligandability

Cysteine 77 of Interleukin-23 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 89 of Interleukin-23 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-23 subunit alpha between cysteines 73 and 77 (54 and 58 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
3d87
Structure name
crystal structure of interleukin-23
Structure deposition date
2008-05-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
9
% buried
52
Peptide accession
Q9NPF7
Residue number A
73
Residue number B
77
Peptide name
Interleukin-23 subunit alpha

Ligandability

Cysteine 73 of Interleukin-23 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 77 of Interleukin-23 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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