ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Dipeptidyl peptidase 1

Intramolecular
Cysteine 321 and cysteine 337
Cysteine 30 and cysteine 118
Cysteine 54 and cysteine 136 L
Cysteine 291 and cysteine 331
Cysteine 255 and cysteine 298
Cysteine 255 and cysteine 258 L
Cysteine 291 and cysteine 321
Cysteine 321 and cysteine 331
Cysteine 257 and cysteine 297 L
A redox-regulated disulphide may form within Dipeptidyl peptidase 1 between cysteines 321 and 337 (297 and 313 respectively in this structure).

Details

Redox score ?
87
PDB code
6ic5
Structure name
human cathepsin-c in complex with dipeptidyl cyclopropyl nitrile inhibitor 2
Structure deposition date
2018-12-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
P53634
Residue number A
321
Residue number B
337
Peptide name
Dipeptidyl peptidase 1

Ligandability

Cysteine 321 of Dipeptidyl peptidase 1

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 337 of Dipeptidyl peptidase 1

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 Dipeptidyl peptidase 1 between cysteines 30 and 118 (6 and 94 respectively in this structure).

Details

Redox score ?
85
PDB code
3pdf
Structure name
discovery of novel cyanamide-based inhibitors of cathepsin c
Structure deposition date
2010-10-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P53634
Residue number A
30
Residue number B
118
Peptide name
Dipeptidyl peptidase 1

Ligandability

Cysteine 30 of Dipeptidyl peptidase 1

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 118 of Dipeptidyl peptidase 1

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 Dipeptidyl peptidase 1 between cysteines 54 and 136 (30 and 112 respectively in this structure).

Details

Redox score ?
84
PDB code
4oel
Structure name
crystal structure of cathepsin c in complex with dipeptide substrates
Structure deposition date
2014-01-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P53634
Residue number A
54
Residue number B
136
Peptide name
Dipeptidyl peptidase 1

Ligandability

Cysteine 54 of Dipeptidyl peptidase 1

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 136 of Dipeptidyl peptidase 1

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.

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 Dipeptidyl peptidase 1 between cysteines 291 and 331 (267 and 307 respectively in this structure).

Details

Redox score ?
83
PDB code
6rn9
Structure name
dpp1 in complex with inhibitor
Structure deposition date
2019-05-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
P53634
Residue number A
291
Residue number B
331
Peptide name
Dipeptidyl peptidase 1

Ligandability

Cysteine 291 of Dipeptidyl peptidase 1

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 331 of Dipeptidyl peptidase 1

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 Dipeptidyl peptidase 1 between cysteines 255 and 298 (231 and 274 respectively in this structure).

Details

Redox score ?
79
PDB code
6rn6
Structure name
dpp1 in complex with inhibitor
Structure deposition date
2019-05-08
Thiol separation (Å)
3
Half-sphere exposure sum ?
61
Minimum pKa ?
9
% buried
33
Peptide accession
P53634
Residue number A
255
Residue number B
298
Peptide name
Dipeptidyl peptidase 1

Ligandability

Cysteine 255 of Dipeptidyl peptidase 1

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 298 of Dipeptidyl peptidase 1

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 Dipeptidyl peptidase 1 between cysteines 255 and 258 (231 and 234 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2djg
Structure name
re-determination of the native structure of human dipeptidyl peptidase i (cathepsin c)
Structure deposition date
2006-04-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
nan
Peptide accession
P53634
Residue number A
255
Residue number B
258
Peptide name
Dipeptidyl peptidase 1

Ligandability

Cysteine 255 of Dipeptidyl peptidase 1

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 258 of Dipeptidyl peptidase 1

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 Dipeptidyl peptidase 1 between cysteines 291 and 321 (267 and 297 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
6rn6
Structure name
dpp1 in complex with inhibitor
Structure deposition date
2019-05-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
52
Minimum pKa ?
11
% buried
36
Peptide accession
P53634
Residue number A
291
Residue number B
321
Peptide name
Dipeptidyl peptidase 1

Ligandability

Cysteine 291 of Dipeptidyl peptidase 1

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 321 of Dipeptidyl peptidase 1

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 Dipeptidyl peptidase 1 between cysteines 321 and 331 (297 and 307 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
4cde
Structure name
human dpp1 in complex with 4-amino-n-((1s)-1-cyano-2-(4-(4- cyanophenyl)phenyl)ethyl)tetrahydropyran-4-carboxamide
Structure deposition date
2013-10-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
P53634
Residue number A
321
Residue number B
331
Peptide name
Dipeptidyl peptidase 1

Ligandability

Cysteine 321 of Dipeptidyl peptidase 1

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 331 of Dipeptidyl peptidase 1

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 Dipeptidyl peptidase 1 between cysteines 257 and 297 (233 and 273 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
1jqp
Structure name
dipeptidyl peptidase i (cathepsin c), a tetrameric cysteine protease of the papain family
Structure deposition date
2001-08-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
7
% buried
nan
Peptide accession
P80067
Residue number A
257
Residue number B
297
Peptide name
Dipeptidyl peptidase 1

Ligandability

Cysteine 257 of Dipeptidyl peptidase 1

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 297 of Dipeptidyl peptidase 1

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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