ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Prolyl endopeptidase-like

Intramolecular
Cysteine 507 and cysteine 538
Cysteine 127 and cysteine 128
Cysteine 160 and cysteine 184
Cysteine 391 and cysteine 409
Cysteine 359 and cysteine 404
A redox-regulated disulphide may form within Prolyl endopeptidase-like between cysteines 507 and 538.

Details

Redox score ?
68
PDB code
7obm
Structure name
crystal structure of the human prolyl endopeptidase-like protein short form (residues 90-727)
Structure deposition date
2021-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
87
Minimum pKa ?
9
% buried
100
Peptide accession
Q4J6C6
Residue number A
507
Residue number B
538
Peptide name
Prolyl endopeptidase-like

Ligandability

Cysteine 507 of Prolyl endopeptidase-like

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 538 of Prolyl endopeptidase-like

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 Prolyl endopeptidase-like between cysteines 127 and 128. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
7obm
Structure name
crystal structure of the human prolyl endopeptidase-like protein short form (residues 90-727)
Structure deposition date
2021-04-22
Thiol separation (Å)
7
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
14
Peptide accession
Q4J6C6
Residue number A
127
Residue number B
128
Peptide name
Prolyl endopeptidase-like

Ligandability

Cysteine 127 of Prolyl endopeptidase-like

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 128 of Prolyl endopeptidase-like

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 Prolyl endopeptidase-like between cysteines 160 and 184. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
7obm
Structure name
crystal structure of the human prolyl endopeptidase-like protein short form (residues 90-727)
Structure deposition date
2021-04-22
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
9
% buried
98
Peptide accession
Q4J6C6
Residue number A
160
Residue number B
184
Peptide name
Prolyl endopeptidase-like

Ligandability

Cysteine 160 of Prolyl endopeptidase-like

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 184 of Prolyl endopeptidase-like

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 Prolyl endopeptidase-like between cysteines 391 and 409. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7obm
Structure name
crystal structure of the human prolyl endopeptidase-like protein short form (residues 90-727)
Structure deposition date
2021-04-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
86
Peptide accession
Q4J6C6
Residue number A
391
Residue number B
409
Peptide name
Prolyl endopeptidase-like

Ligandability

Cysteine 391 of Prolyl endopeptidase-like

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 409 of Prolyl endopeptidase-like

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 Prolyl endopeptidase-like between cysteines 359 and 404. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
7obm
Structure name
crystal structure of the human prolyl endopeptidase-like protein short form (residues 90-727)
Structure deposition date
2021-04-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
13
% buried
96
Peptide accession
Q4J6C6
Residue number A
359
Residue number B
404
Peptide name
Prolyl endopeptidase-like

Ligandability

Cysteine 359 of Prolyl endopeptidase-like

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 404 of Prolyl endopeptidase-like

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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