ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Phospholipase A-2-activating protein

Intramolecular
Cysteine 631 and cysteine 666
Cysteine 787 and cysteine 788
Cysteine 712 and cysteine 725
Cysteine 664 and cysteine 666
Cysteine 666 and cysteine 712
A redox-regulated disulphide may form within Phospholipase A-2-activating protein between cysteines 631 and 666.

Details

Redox score ?
69
PDB code
3ebb
Structure name
plap/p97 complex
Structure deposition date
2008-08-27
Thiol separation (Å)
5
Half-sphere exposure sum ?
80
Minimum pKa ?
8
% buried
90
Peptide accession
Q9Y263
Residue number A
631
Residue number B
666
Peptide name
Phospholipase A-2-activating protein

Ligandability

Cysteine 631 of Phospholipase A-2-activating 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 666 of Phospholipase A-2-activating 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 Phospholipase A-2-activating protein between cysteines 787 and 788. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
3ebb
Structure name
plap/p97 complex
Structure deposition date
2008-08-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
10
% buried
75
Peptide accession
Q9Y263
Residue number A
787
Residue number B
788
Peptide name
Phospholipase A-2-activating protein

Ligandability

Cysteine 787 of Phospholipase A-2-activating 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 788 of Phospholipase A-2-activating 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 Phospholipase A-2-activating protein between cysteines 712 and 725. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
3ebb
Structure name
plap/p97 complex
Structure deposition date
2008-08-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
86
Peptide accession
Q9Y263
Residue number A
712
Residue number B
725
Peptide name
Phospholipase A-2-activating protein

Ligandability

Cysteine 712 of Phospholipase A-2-activating 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 725 of Phospholipase A-2-activating 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 Phospholipase A-2-activating protein between cysteines 664 and 666. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
3ebb
Structure name
plap/p97 complex
Structure deposition date
2008-08-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
84
Minimum pKa ?
13
% buried
100
Peptide accession
Q9Y263
Residue number A
664
Residue number B
666
Peptide name
Phospholipase A-2-activating protein

Ligandability

Cysteine 664 of Phospholipase A-2-activating 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 666 of Phospholipase A-2-activating 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 Phospholipase A-2-activating protein between cysteines 666 and 712. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
3ebb
Structure name
plap/p97 complex
Structure deposition date
2008-08-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
88
Peptide accession
Q9Y263
Residue number A
666
Residue number B
712
Peptide name
Phospholipase A-2-activating protein

Ligandability

Cysteine 666 of Phospholipase A-2-activating 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 712 of Phospholipase A-2-activating 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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