ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Tripeptidyl-peptidase 1

Intramolecular
Cysteine 111 and cysteine 122
Cysteine 365 and cysteine 526 L
Cysteine 522 and cysteine 537
A redox-regulated disulphide may form within Tripeptidyl-peptidase 1 between cysteines 111 and 122.

Details

Redox score ?
86
PDB code
3edy
Structure name
crystal structure of the precursor form of human tripeptidyl-peptidase 1
Structure deposition date
2008-09-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14773
Residue number A
111
Residue number B
122
Peptide name
Tripeptidyl-peptidase 1

Ligandability

Cysteine 111 of Tripeptidyl-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 122 of Tripeptidyl-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 Tripeptidyl-peptidase 1 between cysteines 365 and 526.

Details

Redox score ?
81
PDB code
3ee6
Structure name
crystal structure analysis of tripeptidyl peptidase -i
Structure deposition date
2008-09-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14773
Residue number A
365
Residue number B
526
Peptide name
Tripeptidyl-peptidase 1

Ligandability

Cysteine 365 of Tripeptidyl-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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 526 of Tripeptidyl-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 Tripeptidyl-peptidase 1 between cysteines 522 and 537.

Details

Redox score ?
76
PDB code
3edy
Structure name
crystal structure of the precursor form of human tripeptidyl-peptidase 1
Structure deposition date
2008-09-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14773
Residue number A
522
Residue number B
537
Peptide name
Tripeptidyl-peptidase 1

Ligandability

Cysteine 522 of Tripeptidyl-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 537 of Tripeptidyl-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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