ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Lymphotactin

Intramolecular
Cysteine 32 and cysteine 69 L
Cysteine 32 and cysteine 236 L
Cysteine 69 and cysteine 249 L
Cysteine 32 and cysteine 249 L
A redox-regulated disulphide may form within Lymphotactin between cysteines 32 and 69 (11 and 48 respectively in this structure).

Details

Redox score ?
80
PDB code
2nyz
Structure name
viral chemokine binding protein m3 from murine gammaherpesvirus68 in complex with the c- chemokine xcl1
Structure deposition date
2006-11-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
P47992
Residue number A
32
Residue number B
69
Peptide name
Lymphotactin

Ligandability

Cysteine 32 of Lymphotactin

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.

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 69 of Lymphotactin

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.

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 Lymphotactin between cysteines 32 and 236 (211 and 236 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
2n54
Structure name
solution structure of a disulfide stabilized xcl1 dimer
Structure deposition date
2015-07-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P47992
Residue number A
32
Residue number B
236
Peptide name
Lymphotactin

Ligandability

Cysteine 32 of Lymphotactin

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.

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 236 of Lymphotactin

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.

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 236 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Lymphotactin between cysteines 69 and 249 (248 and 249 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
2n54
Structure name
solution structure of a disulfide stabilized xcl1 dimer
Structure deposition date
2015-07-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P47992
Residue number A
69
Residue number B
249
Peptide name
Lymphotactin

Ligandability

Cysteine 69 of Lymphotactin

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.

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 249 of Lymphotactin

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 249 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Lymphotactin between cysteines 32 and 249 (211 and 249 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
2n54
Structure name
solution structure of a disulfide stabilized xcl1 dimer
Structure deposition date
2015-07-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P47992
Residue number A
32
Residue number B
249
Peptide name
Lymphotactin

Ligandability

Cysteine 32 of Lymphotactin

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.

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 249 of Lymphotactin

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 249 in protein B could not be asigned to a Uniprot residue.
If this tool was useful for finding a disulphide, please cite: