ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Kallikrein-8

Intramolecular
Cysteine 152 and cysteine 218
Cysteine 39 and cysteine 173
Cysteine 145 and cysteine 246
Cysteine 184 and cysteine 198
Cysteine 58 and cysteine 74
Cysteine 208 and cysteine 233
Cysteine 218 and cysteine 246
A redox-regulated disulphide may form within Kallikrein-8 between cysteines 152 and 218 (136 and 201 respectively in this structure).

Details

Redox score ?
85
PDB code
5ms4
Structure name
kallikrein-related peptidase 8 leupeptin inhibitor complex
Structure deposition date
2016-12-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60259
Residue number A
152
Residue number B
218
Peptide name
Kallikrein-8

Ligandability

Cysteine 152 of Kallikrein-8

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 218 of Kallikrein-8

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 Kallikrein-8 between cysteines 39 and 173 (22 and 157 respectively in this structure).

Details

Redox score ?
84
PDB code
5ms4
Structure name
kallikrein-related peptidase 8 leupeptin inhibitor complex
Structure deposition date
2016-12-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60259
Residue number A
39
Residue number B
173
Peptide name
Kallikrein-8

Ligandability

Cysteine 39 of Kallikrein-8

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 173 of Kallikrein-8

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 Kallikrein-8 between cysteines 145 and 246 (129 and 232 respectively in this structure).

Details

Redox score ?
82
PDB code
5ms4
Structure name
kallikrein-related peptidase 8 leupeptin inhibitor complex
Structure deposition date
2016-12-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60259
Residue number A
145
Residue number B
246
Peptide name
Kallikrein-8

Ligandability

Cysteine 145 of Kallikrein-8

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 246 of Kallikrein-8

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 Kallikrein-8 between cysteines 184 and 198 (168 and 182 respectively in this structure).

Details

Redox score ?
82
PDB code
5ms4
Structure name
kallikrein-related peptidase 8 leupeptin inhibitor complex
Structure deposition date
2016-12-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60259
Residue number A
184
Residue number B
198
Peptide name
Kallikrein-8

Ligandability

Cysteine 184 of Kallikrein-8

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 198 of Kallikrein-8

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 Kallikrein-8 between cysteines 58 and 74 (42 and 58 respectively in this structure).

Details

Redox score ?
81
PDB code
5ms4
Structure name
kallikrein-related peptidase 8 leupeptin inhibitor complex
Structure deposition date
2016-12-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60259
Residue number A
58
Residue number B
74
Peptide name
Kallikrein-8

Ligandability

Cysteine 58 of Kallikrein-8

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 74 of Kallikrein-8

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 Kallikrein-8 between cysteines 208 and 233 (191 and 220 respectively in this structure).

Details

Redox score ?
80
PDB code
5ms4
Structure name
kallikrein-related peptidase 8 leupeptin inhibitor complex
Structure deposition date
2016-12-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60259
Residue number A
208
Residue number B
233
Peptide name
Kallikrein-8

Ligandability

Cysteine 208 of Kallikrein-8

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 233 of Kallikrein-8

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 Kallikrein-8 between cysteines 218 and 246 (201 and 232 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5ms4
Structure name
kallikrein-related peptidase 8 leupeptin inhibitor complex
Structure deposition date
2016-12-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60259
Residue number A
218
Residue number B
246
Peptide name
Kallikrein-8

Ligandability

Cysteine 218 of Kallikrein-8

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 246 of Kallikrein-8

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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