ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Peptidyl-prolyl cis-trans isomerase-like 3

Intramolecular
Cysteine 18 and cysteine 25
Cysteine 25 and cysteine 32
A redox-regulated disulphide may form within Peptidyl-prolyl cis-trans isomerase-like 3 between cysteines 18 and 25 (24 and 31 respectively in this structure).

Details

Redox score ?
83
PDB code
2oju
Structure name
x-ray structure of complex of human cyclophilin j with cyclosporin a
Structure deposition date
2007-01-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H2H8
Residue number A
18
Residue number B
25
Peptide name
Peptidyl-prolyl cis-trans isomerase-like 3

Ligandability

Cysteine 18 of Peptidyl-prolyl cis-trans isomerase-like 3

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 25 of Peptidyl-prolyl cis-trans isomerase-like 3

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 Peptidyl-prolyl cis-trans isomerase-like 3 between cysteines 25 and 32. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
2ok3
Structure name
x-ray structure of human cyclophilin j at 2
Structure deposition date
2007-01-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
13
% buried
nan
Peptide accession
Q9H2H8
Residue number A
25
Residue number B
32
Peptide name
Peptidyl-prolyl cis-trans isomerase-like 3

Ligandability

Cysteine 25 of Peptidyl-prolyl cis-trans isomerase-like 3

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 32 of Peptidyl-prolyl cis-trans isomerase-like 3

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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