ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Mixed lineage kinase domain-like protein

Intramolecular
Cysteine 18 and cysteine 28
Cysteine 24 and cysteine 28
Cysteine 24 and cysteine 86
Cysteine 18 and cysteine 24
A redox-regulated disulphide may form within Mixed lineage kinase domain-like protein between cysteines 18 and 28. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
6ux8
Structure name
structure of monobody 33 mlkl n-terminal domain complex
Structure deposition date
2019-11-07
Thiol separation (Å)
6
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
75
Peptide accession
Q8NB16
Residue number A
18
Residue number B
28
Peptide name
Mixed lineage kinase domain-like protein

Ligandability

Cysteine 18 of Mixed lineage kinase domain-like protein

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 28 of Mixed lineage kinase domain-like protein

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 Mixed lineage kinase domain-like protein between cysteines 24 and 28. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
6ux8
Structure name
structure of monobody 33 mlkl n-terminal domain complex
Structure deposition date
2019-11-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
68
Peptide accession
Q8NB16
Residue number A
24
Residue number B
28
Peptide name
Mixed lineage kinase domain-like protein

Ligandability

Cysteine 24 of Mixed lineage kinase domain-like protein

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 28 of Mixed lineage kinase domain-like protein

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 Mixed lineage kinase domain-like protein between cysteines 24 and 86. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7nm2
Structure name
solution structure of mlkl executioner domain in complex with a fragment
Structure deposition date
2021-02-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
9
% buried
40
Peptide accession
Q8NB16
Residue number A
24
Residue number B
86
Peptide name
Mixed lineage kinase domain-like protein

Ligandability

Cysteine 24 of Mixed lineage kinase domain-like protein

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 86 of Mixed lineage kinase domain-like protein

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 Mixed lineage kinase domain-like protein between cysteines 18 and 24. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
2msv
Structure name
solution structure of the mlkl n-terminal domain
Structure deposition date
2014-08-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
78
Peptide accession
Q8NB16
Residue number A
18
Residue number B
24
Peptide name
Mixed lineage kinase domain-like protein

Ligandability

Cysteine 18 of Mixed lineage kinase domain-like protein

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 24 of Mixed lineage kinase domain-like protein

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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