ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Prolyl endopeptidase

Intramolecular
Cysteine 78 and cysteine 343 L
Cysteine 255 and cysteine 264
Cysteine 573 and cysteine 703
Cysteine 57 and cysteine 703 L
Cysteine 225 and cysteine 264
Cysteine 526 and cysteine 563 L
Cysteine 532 and cysteine 563 L
Cysteine 175 and cysteine 225 L
Cysteine 73 and cysteine 703 L
A redox-regulated disulphide may form within Prolyl endopeptidase between cysteines 78 and 343 (78 and 397 respectively in this structure).

Details

Redox score ?
82
PDB code
1e5t
Structure name
prolyl oligopeptidase from porcine brain, mutant
Structure deposition date
2000-08-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P23687
Residue number A
78
Residue number B
343
Peptide name
Prolyl endopeptidase

Ligandability

Cysteine 78 of Prolyl endopeptidase

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 343 of Prolyl endopeptidase

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Prolyl endopeptidase between cysteines 255 and 264 (255 and 597 respectively in this structure).

Details

Redox score ?
81
PDB code
1vz3
Structure name
prolyl oligopeptidase from porcine brain, t597c mutant
Structure deposition date
2004-05-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P23687
Residue number A
255
Residue number B
264
Peptide name
Prolyl endopeptidase

Ligandability

Cysteine 255 of Prolyl endopeptidase

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 264 of Prolyl endopeptidase

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.

Uncertain whether structure cysteine 597 has been assigned to correct residue.
A redox-regulated disulphide may form within Prolyl endopeptidase between cysteines 573 and 703. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
3ddu
Structure name
prolyl oligopeptidase with gsk552
Structure deposition date
2008-06-06
Thiol separation (Å)
5
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
99
Peptide accession
P48147
Residue number A
573
Residue number B
703
Peptide name
Prolyl endopeptidase

Ligandability

Cysteine 573 of Prolyl endopeptidase

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 703 of Prolyl endopeptidase

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 between cysteines 57 and 703. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3ddu
Structure name
prolyl oligopeptidase with gsk552
Structure deposition date
2008-06-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
74
Peptide accession
P48147
Residue number A
57
Residue number B
703
Peptide name
Prolyl endopeptidase

Ligandability

Cysteine 57 of Prolyl endopeptidase

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 703 of Prolyl endopeptidase

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 between cysteines 225 and 264. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
3ddu
Structure name
prolyl oligopeptidase with gsk552
Structure deposition date
2008-06-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
12
% buried
72
Peptide accession
P48147
Residue number A
225
Residue number B
264
Peptide name
Prolyl endopeptidase

Ligandability

Cysteine 225 of Prolyl endopeptidase

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 264 of Prolyl endopeptidase

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 between cysteines 526 and 563. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
3ddu
Structure name
prolyl oligopeptidase with gsk552
Structure deposition date
2008-06-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
89
Minimum pKa ?
11
% buried
100
Peptide accession
P48147
Residue number A
526
Residue number B
563
Peptide name
Prolyl endopeptidase

Ligandability

Cysteine 526 of Prolyl endopeptidase

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 563 of Prolyl endopeptidase

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 between cysteines 532 and 563. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
3ddu
Structure name
prolyl oligopeptidase with gsk552
Structure deposition date
2008-06-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
74
Peptide accession
P48147
Residue number A
532
Residue number B
563
Peptide name
Prolyl endopeptidase

Ligandability

Cysteine 532 of Prolyl endopeptidase

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 563 of Prolyl endopeptidase

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 between cysteines 175 and 225. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
1uoo
Structure name
prolyl oligopeptidase from porcine brain, s554a mutant with bound peptide ligand gly-phe-arg-pro
Structure deposition date
2003-09-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
92
Peptide accession
P23687
Residue number A
175
Residue number B
225
Peptide name
Prolyl endopeptidase

Ligandability

Cysteine 175 of Prolyl endopeptidase

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 225 of Prolyl endopeptidase

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 between cysteines 73 and 703 (73 and 427 respectively in this structure).

Details

Redox score ?
nan
PDB code
1vz2
Structure name
prolyl oligopeptidase from porcine brain, y73c/v427c/c255t mutant
Structure deposition date
2004-05-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
41
Minimum pKa ?
nan
% buried
nan
Peptide accession
P23687
Residue number A
73
Residue number B
703
Peptide name
Prolyl endopeptidase

Ligandability

Cysteine 73 of Prolyl endopeptidase

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 703 of Prolyl endopeptidase

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 73 in protein A could not be asigned to a Uniprot residue.
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