ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Leukemia inhibitory factor receptor

Intramolecular
Cysteine 55 and cysteine 65
Cysteine 341 and cysteine 351
Cysteine 82 and cysteine 90
Cysteine 466 and cysteine 511
Cysteine 213 and cysteine 270
Cysteine 213 and cysteine 271
Cysteine 270 and cysteine 271
A redox-regulated disulphide may form within Leukemia inhibitory factor receptor between cysteines 55 and 65 (4 and 14 respectively in this structure).

Details

Redox score ?
86
PDB code
3e0g
Structure name
structure of the leukemia inhibitory factor receptor (lif-r) domains d1-d5
Structure deposition date
2008-07-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P42702
Residue number A
55
Residue number B
65
Peptide name
Leukemia inhibitory factor receptor

Ligandability

Cysteine 55 of Leukemia inhibitory factor receptor

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 65 of Leukemia inhibitory factor receptor

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 Leukemia inhibitory factor receptor between cysteines 341 and 351 (290 and 300 respectively in this structure).

Details

Redox score ?
84
PDB code
3e0g
Structure name
structure of the leukemia inhibitory factor receptor (lif-r) domains d1-d5
Structure deposition date
2008-07-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P42702
Residue number A
341
Residue number B
351
Peptide name
Leukemia inhibitory factor receptor

Ligandability

Cysteine 341 of Leukemia inhibitory factor receptor

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 351 of Leukemia inhibitory factor receptor

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 Leukemia inhibitory factor receptor between cysteines 82 and 90 (31 and 39 respectively in this structure).

Details

Redox score ?
83
PDB code
3e0g
Structure name
structure of the leukemia inhibitory factor receptor (lif-r) domains d1-d5
Structure deposition date
2008-07-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
P42702
Residue number A
82
Residue number B
90
Peptide name
Leukemia inhibitory factor receptor

Ligandability

Cysteine 82 of Leukemia inhibitory factor receptor

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 90 of Leukemia inhibitory factor receptor

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 Leukemia inhibitory factor receptor between cysteines 466 and 511 (415 and 460 respectively in this structure).

Details

Redox score ?
83
PDB code
3e0g
Structure name
structure of the leukemia inhibitory factor receptor (lif-r) domains d1-d5
Structure deposition date
2008-07-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P42702
Residue number A
466
Residue number B
511
Peptide name
Leukemia inhibitory factor receptor

Ligandability

Cysteine 466 of Leukemia inhibitory factor receptor

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 511 of Leukemia inhibitory factor receptor

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 Leukemia inhibitory factor receptor between cysteines 213 and 270 (162 and 219 respectively in this structure).

Details

Redox score ?
78
PDB code
3e0g
Structure name
structure of the leukemia inhibitory factor receptor (lif-r) domains d1-d5
Structure deposition date
2008-07-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P42702
Residue number A
213
Residue number B
270
Peptide name
Leukemia inhibitory factor receptor

Ligandability

Cysteine 213 of Leukemia inhibitory factor receptor

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 270 of Leukemia inhibitory factor receptor

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 Leukemia inhibitory factor receptor between cysteines 213 and 271 (162 and 220 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
3e0g
Structure name
structure of the leukemia inhibitory factor receptor (lif-r) domains d1-d5
Structure deposition date
2008-07-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
88
Minimum pKa ?
12
% buried
nan
Peptide accession
P42702
Residue number A
213
Residue number B
271
Peptide name
Leukemia inhibitory factor receptor

Ligandability

Cysteine 213 of Leukemia inhibitory factor receptor

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 271 of Leukemia inhibitory factor receptor

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 Leukemia inhibitory factor receptor between cysteines 270 and 271 (219 and 220 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
3e0g
Structure name
structure of the leukemia inhibitory factor receptor (lif-r) domains d1-d5
Structure deposition date
2008-07-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
nan
Peptide accession
P42702
Residue number A
270
Residue number B
271
Peptide name
Leukemia inhibitory factor receptor

Ligandability

Cysteine 270 of Leukemia inhibitory factor receptor

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 271 of Leukemia inhibitory factor receptor

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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