ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Peptidyl-prolyl cis-trans isomerase E

Intramolecular
Cysteine 198 and cysteine 252
Cysteine 176 and cysteine 297
Cysteine 174 and cysteine 176
Cysteine 252 and cysteine 8
Cysteine 38 and cysteine 41
A redox-regulated disulphide may form within Peptidyl-prolyl cis-trans isomerase E between cysteines 198 and 252.

Details

Redox score ?
78
PDB code
3uch
Structure name
crystal structure of a peptidyl-prolyl cis-trans isomerase e (ppie) from homo sapiens at 2
Structure deposition date
2011-10-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
8
% buried
78
Peptide accession
Q9UNP9
Residue number A
198
Residue number B
252
Peptide name
Peptidyl-prolyl cis-trans isomerase E

Ligandability

Cysteine 198 of Peptidyl-prolyl cis-trans isomerase E

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 252 of Peptidyl-prolyl cis-trans isomerase E

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 E between cysteines 176 and 297.

Details

Redox score ?
61
PDB code
3uch
Structure name
crystal structure of a peptidyl-prolyl cis-trans isomerase e (ppie) from homo sapiens at 2
Structure deposition date
2011-10-26
Thiol separation (Å)
5
Half-sphere exposure sum ?
70
Minimum pKa ?
12
% buried
86
Peptide accession
Q9UNP9
Residue number A
176
Residue number B
297
Peptide name
Peptidyl-prolyl cis-trans isomerase E

Ligandability

Cysteine 176 of Peptidyl-prolyl cis-trans isomerase E

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 297 of Peptidyl-prolyl cis-trans isomerase E

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 E between cysteines 174 and 176. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
2r99
Structure name
crystal structure of cyclophilin abh-like domain of human peptidylprolyl isomerase e isoform 1
Structure deposition date
2007-09-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
65
Peptide accession
Q9UNP9
Residue number A
174
Residue number B
176
Peptide name
Peptidyl-prolyl cis-trans isomerase E

Ligandability

Cysteine 174 of Peptidyl-prolyl cis-trans isomerase E

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 176 of Peptidyl-prolyl cis-trans isomerase E

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 E between cysteines 252 and 8 (5 and 8 respectively in this structure).

Details

Redox score ?
nan
PDB code
2ku7
Structure name
solution structure of mll1 phd3-cyp33 rrm chimeric protein
Structure deposition date
2010-02-12
Thiol separation (Å)
6
Half-sphere exposure sum ?
16
Minimum pKa ?
9
% buried
0
Peptide accession
Q9UNP9
Residue number A
252
Residue number B
8
Peptide name
Peptidyl-prolyl cis-trans isomerase E

Ligandability

Cysteine 252 of Peptidyl-prolyl cis-trans isomerase E

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 8 of Peptidyl-prolyl cis-trans isomerase E

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 8 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Peptidyl-prolyl cis-trans isomerase E between cysteines 38 and 41.

Details

Redox score ?
nan
PDB code
2ku7
Structure name
solution structure of mll1 phd3-cyp33 rrm chimeric protein
Structure deposition date
2010-02-12
Thiol separation (Å)
5
Half-sphere exposure sum ?
21
Minimum pKa ?
9
% buried
0
Peptide accession
Q9UNP9
Residue number A
38
Residue number B
41
Peptide name
Peptidyl-prolyl cis-trans isomerase E

Ligandability

Cysteine 38 of Peptidyl-prolyl cis-trans isomerase E

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 Peptidyl-prolyl cis-trans isomerase E

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 38 in protein A could not be asigned to a Uniprot residue.
Cysteine 41 in protein B could not be asigned to a Uniprot residue.
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