ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Dipeptidyl peptidase 9

Intermolecular
Cysteine 844 and cysteine 1288 of NACHT, LRR and PYD domains-containing protein 1 L
Intramolecular
Cysteine 194 and cysteine 259
Cysteine 447 and cysteine 452
Cysteine 452 and cysteine 683
A redox-regulated disulphide may form between cysteine 844 of Dipeptidyl peptidase 9 and cysteine 1288 of NACHT, LRR and PYD domains-containing protein 1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
6x6a
Structure name
cryo-em structure of nlrp1-dpp9 complex
Structure deposition date
2020-05-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
12
% buried
88
Peptide A name
Dipeptidyl peptidase 9
Peptide B name
NACHT, LRR and PYD domains-containing protein 1
Peptide A accession
Q86TI2
Peptide B accession
Q9C000
Peptide A residue number
844
Peptide B residue number
1288

Ligandability

Cysteine 844 of Dipeptidyl peptidase 9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

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 1288 of NACHT, LRR and PYD domains-containing protein 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 9 between cysteines 194 and 259. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
7svl
Structure name
dpp9 in complex with ligand iced-2
Structure deposition date
2021-11-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
91
Peptide accession
Q86TI2
Residue number A
194
Residue number B
259
Peptide name
Dipeptidyl peptidase 9

Ligandability

Cysteine 194 of Dipeptidyl peptidase 9

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 259 of Dipeptidyl peptidase 9

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 9 between cysteines 447 and 452. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
6eor
Structure name
dpp9 - 1g244
Structure deposition date
2017-10-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
14
% buried
92
Peptide accession
Q86TI2
Residue number A
447
Residue number B
452
Peptide name
Dipeptidyl peptidase 9

Ligandability

Cysteine 447 of Dipeptidyl peptidase 9

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 452 of Dipeptidyl peptidase 9

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 9 between cysteines 452 and 683. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
7a3f
Structure name
crystal structure of apo dpp9
Structure deposition date
2020-08-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
99
Peptide accession
Q86TI2
Residue number A
452
Residue number B
683
Peptide name
Dipeptidyl peptidase 9

Ligandability

Cysteine 452 of Dipeptidyl peptidase 9

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 683 of Dipeptidyl peptidase 9

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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