ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Leukemia inhibitory factor

Intramolecular
Cysteine 35 and cysteine 157
Cysteine 82 and cysteine 185
Cysteine 40 and cysteine 153 L
Cysteine 40 and cysteine 156
Cysteine 153 and cysteine 156 L
Cysteine 35 and cysteine 41
Cysteine 34 and cysteine 153 L
A redox-regulated disulphide may form within Leukemia inhibitory factor between cysteines 35 and 157 (12 and 134 respectively in this structure).

Details

Redox score ?
86
PDB code
1lki
Structure name
the crystal structure and biological function of leukemia inhibitory factor: implications for receptor binding
Structure deposition date
1994-12-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09056
Residue number A
35
Residue number B
157
Peptide name
Leukemia inhibitory factor

Ligandability

Cysteine 35 of Leukemia inhibitory factor

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 157 of Leukemia inhibitory factor

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 between cysteines 82 and 185 (60 and 163 respectively in this structure).

Details

Redox score ?
84
PDB code
7n0a
Structure name
structure of human leukaemia inhibitory factor with fab msc1
Structure deposition date
2021-05-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15018
Residue number A
82
Residue number B
185
Peptide name
Leukemia inhibitory factor

Ligandability

Cysteine 82 of Leukemia inhibitory factor

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 185 of Leukemia inhibitory factor

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 between cysteines 40 and 153 (18 and 131 respectively in this structure).

Details

Redox score ?
82
PDB code
7n0a
Structure name
structure of human leukaemia inhibitory factor with fab msc1
Structure deposition date
2021-05-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15018
Residue number A
40
Residue number B
153
Peptide name
Leukemia inhibitory factor

Ligandability

Cysteine 40 of Leukemia inhibitory factor

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 153 of Leukemia inhibitory factor

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 Leukemia inhibitory factor between cysteines 40 and 156 (18 and 134 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
1pvh
Structure name
crystal structure of leukemia inhibitory factor in complex with gp130
Structure deposition date
2003-06-27
Thiol separation (Å)
7
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15018
Residue number A
40
Residue number B
156
Peptide name
Leukemia inhibitory factor

Ligandability

Cysteine 40 of Leukemia inhibitory factor

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 156 of Leukemia inhibitory factor

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 between cysteines 153 and 156 (132 and 135 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
1emr
Structure name
crystal structure of human leukemia inhibitory factor (lif)
Structure deposition date
2000-03-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
0
Peptide accession
P15018
Residue number A
153
Residue number B
156
Peptide name
Leukemia inhibitory factor

Ligandability

Cysteine 153 of Leukemia inhibitory factor

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 156 of Leukemia inhibitory factor

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 between cysteines 35 and 41 (12 and 18 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
1lki
Structure name
the crystal structure and biological function of leukemia inhibitory factor: implications for receptor binding
Structure deposition date
1994-12-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09056
Residue number A
35
Residue number B
41
Peptide name
Leukemia inhibitory factor

Ligandability

Cysteine 35 of Leukemia inhibitory factor

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 41 of Leukemia inhibitory factor

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 between cysteines 34 and 153 (12 and 131 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
2q7n
Structure name
crystal structure of leukemia inhibitory factor in complex with lif receptor (domains 1-5)
Structure deposition date
2007-06-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15018
Residue number A
34
Residue number B
153
Peptide name
Leukemia inhibitory factor

Ligandability

Cysteine 34 of Leukemia inhibitory factor

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 153 of Leukemia inhibitory factor

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.

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