ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Tumor necrosis factor ligand superfamily member 12

Intramolecular
Cysteine 191 and cysteine 210
Cysteine 165 and cysteine 210
Cysteine 165 and cysteine 191
A redox-regulated disulphide may form within Tumor necrosis factor ligand superfamily member 12 between cysteines 191 and 210 (96 and 115 respectively in this structure).

Details

Redox score ?
82
PDB code
4ht1
Structure name
human tweak in complex with the fab fragment of a neutralizing antibody
Structure deposition date
2012-10-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43508
Residue number A
191
Residue number B
210
Peptide name
Tumor necrosis factor ligand superfamily member 12

Ligandability

Cysteine 191 of Tumor necrosis factor ligand superfamily member 12

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 210 of Tumor necrosis factor ligand superfamily member 12

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 Tumor necrosis factor ligand superfamily member 12 between cysteines 165 and 210 (70 and 115 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
4ht1
Structure name
human tweak in complex with the fab fragment of a neutralizing antibody
Structure deposition date
2012-10-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
12
% buried
nan
Peptide accession
O43508
Residue number A
165
Residue number B
210
Peptide name
Tumor necrosis factor ligand superfamily member 12

Ligandability

Cysteine 165 of Tumor necrosis factor ligand superfamily member 12

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 210 of Tumor necrosis factor ligand superfamily member 12

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 Tumor necrosis factor ligand superfamily member 12 between cysteines 165 and 191 (70 and 96 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
4ht1
Structure name
human tweak in complex with the fab fragment of a neutralizing antibody
Structure deposition date
2012-10-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
12
% buried
nan
Peptide accession
O43508
Residue number A
165
Residue number B
191
Peptide name
Tumor necrosis factor ligand superfamily member 12

Ligandability

Cysteine 165 of Tumor necrosis factor ligand superfamily member 12

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 191 of Tumor necrosis factor ligand superfamily member 12

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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