ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Pleckstrin homology domain-containing family M member 2

Intramolecular
Cysteine 829 and cysteine 869 L
Cysteine 826 and cysteine 829 L
Cysteine 826 and cysteine 869
A redox-regulated disulphide may form within Pleckstrin homology domain-containing family M member 2 between cysteines 829 and 869 (830 and 870 respectively in this structure).

Details

Redox score ?
65
PDB code
3cxb
Structure name
crystal structure of sifa and skip
Structure deposition date
2008-04-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
9
% buried
99
Peptide accession
Q8IWE5
Residue number A
829
Residue number B
869
Peptide name
Pleckstrin homology domain-containing family M member 2

Ligandability

Cysteine 829 of Pleckstrin homology domain-containing family M member 2

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 869 of Pleckstrin homology domain-containing family M member 2

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 Pleckstrin homology domain-containing family M member 2 between cysteines 826 and 829 (827 and 830 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
3cxb
Structure name
crystal structure of sifa and skip
Structure deposition date
2008-04-24
Thiol separation (Å)
5
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
86
Peptide accession
Q8IWE5
Residue number A
826
Residue number B
829
Peptide name
Pleckstrin homology domain-containing family M member 2

Ligandability

Cysteine 826 of Pleckstrin homology domain-containing family M member 2

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 829 of Pleckstrin homology domain-containing family M member 2

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Pleckstrin homology domain-containing family M member 2 between cysteines 826 and 869 (827 and 870 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
3cxb
Structure name
crystal structure of sifa and skip
Structure deposition date
2008-04-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
9
% buried
86
Peptide accession
Q8IWE5
Residue number A
826
Residue number B
869
Peptide name
Pleckstrin homology domain-containing family M member 2

Ligandability

Cysteine 826 of Pleckstrin homology domain-containing family M member 2

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 869 of Pleckstrin homology domain-containing family M member 2

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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