ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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peptidylprolyl isomerase

Intramolecular
Cysteine 234 and cysteine 20
Cysteine 234 and cysteine 518
Cysteine 500 and cysteine 20
A redox-regulated disulphide may form within peptidylprolyl isomerase between cysteines 234 and 20 (234 and 519 respectively in this structure).

Details

Redox score ?
nan
PDB code
7epd
Structure name
cryo-em structure of inactive mglu2-7 heterodimer
Structure deposition date
2021-04-26
Thiol separation (Å)
5
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q0VDC6
Residue number A
234
Residue number B
20
Peptide name
peptidylprolyl isomerase

Ligandability

Cysteine 234 of peptidylprolyl isomerase

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 20 of peptidylprolyl isomerase

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 234 in protein A could not be asigned to a Uniprot residue.
Uncertain whether structure cysteine 519 has been assigned to correct residue.
A redox-regulated disulphide may form within peptidylprolyl isomerase between cysteines 234 and 518.

Details

Redox score ?
nan
PDB code
7epd
Structure name
cryo-em structure of inactive mglu2-7 heterodimer
Structure deposition date
2021-04-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q0VDC6
Residue number A
234
Residue number B
518
Peptide name
peptidylprolyl isomerase

Ligandability

Cysteine 234 of peptidylprolyl isomerase

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 518 of peptidylprolyl isomerase

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 234 in protein A could not be asigned to a Uniprot residue.
Cysteine 518 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within peptidylprolyl isomerase between cysteines 500 and 20 (500 and 519 respectively in this structure).

Details

Redox score ?
nan
PDB code
7epd
Structure name
cryo-em structure of inactive mglu2-7 heterodimer
Structure deposition date
2021-04-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q0VDC6
Residue number A
500
Residue number B
20
Peptide name
peptidylprolyl isomerase

Ligandability

Cysteine 500 of peptidylprolyl isomerase

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 20 of peptidylprolyl isomerase

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 500 in protein A could not be asigned to a Uniprot residue.
Uncertain whether structure cysteine 519 has been assigned to correct residue.
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