ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Dipeptidyl peptidase 9

Intramolecular
Cysteine 205 and cysteine 270
Cysteine 458 and cysteine 463
A redox-regulated disulphide may form within Dipeptidyl peptidase 9 between cysteines 205 and 270 (193 and 258 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
7crw
Structure name
cryo-em structure of rnlrp1-rdpp9 complex
Structure deposition date
2020-08-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
78
Peptide accession
M0R781
Residue number A
205
Residue number B
270
Peptide name
Dipeptidyl peptidase 9

Ligandability

Cysteine 205 of Dipeptidyl peptidase 9

Cysteine 270 of Dipeptidyl peptidase 9

A redox-regulated disulphide may form within Dipeptidyl peptidase 9 between cysteines 458 and 463 (446 and 451 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
7crw
Structure name
cryo-em structure of rnlrp1-rdpp9 complex
Structure deposition date
2020-08-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
12
% buried
83
Peptide accession
M0R781
Residue number A
458
Residue number B
463
Peptide name
Dipeptidyl peptidase 9

Ligandability

Cysteine 458 of Dipeptidyl peptidase 9

Cysteine 463 of Dipeptidyl peptidase 9

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