ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Dipeptidase 1

Intermolecular
Cysteine 377 and cysteine 377
Intramolecular
Cysteine 242 and cysteine 274
Cysteine 87 and cysteine 170
A redox-regulated disulphide may form between two units of Dipeptidase 1 at cysteines 377 and 377 (361 and 361 respectively in this structure).

Details

Redox score ?
88
PDB code
1itu
Structure name
human renal dipeptidase complexed with cilastatin
Structure deposition date
2002-02-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide A name
Dipeptidase 1
Peptide B name
Dipeptidase 1
Peptide A accession
P16444
Peptide B accession
P16444
Peptide A residue number
377
Peptide B residue number
377

Ligandability

A redox-regulated disulphide may form within Dipeptidase 1 between cysteines 242 and 274 (226 and 258 respectively in this structure).

Details

Redox score ?
85
PDB code
1itu
Structure name
human renal dipeptidase complexed with cilastatin
Structure deposition date
2002-02-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16444
Residue number A
242
Residue number B
274
Peptide name
Dipeptidase 1

Ligandability

Cysteine 242 of Dipeptidase 1

Cysteine 274 of Dipeptidase 1

A redox-regulated disulphide may form within Dipeptidase 1 between cysteines 87 and 170 (71 and 154 respectively in this structure).

Details

Redox score ?
79
PDB code
1itq
Structure name
human renal dipeptidase
Structure deposition date
2002-02-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16444
Residue number A
87
Residue number B
170
Peptide name
Dipeptidase 1

Ligandability

Cysteine 87 of Dipeptidase 1

Cysteine 170 of Dipeptidase 1

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