ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Kallikrein-10

Intramolecular
Cysteine 52 and cysteine 190
Cysteine 169 and cysteine 235
Cysteine 162 and cysteine 263
Cysteine 71 and cysteine 87
Cysteine 201 and cysteine 215
Cysteine 225 and cysteine 250
Cysteine 235 and cysteine 263
A redox-regulated disulphide may form within Kallikrein-10 between cysteines 52 and 190 (22 and 157 respectively in this structure).

Details

Redox score ?
87
PDB code
5lpf
Structure name
kallikrein-related peptidase 10
Structure deposition date
2016-08-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43240
Residue number A
52
Residue number B
190
Peptide name
Kallikrein-10

Ligandability

Cysteine 52 of Kallikrein-10

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 190 of Kallikrein-10

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-10 between cysteines 169 and 235 (136 and 201 respectively in this structure).

Details

Redox score ?
85
PDB code
5lpf
Structure name
kallikrein-related peptidase 10
Structure deposition date
2016-08-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43240
Residue number A
169
Residue number B
235
Peptide name
Kallikrein-10

Ligandability

Cysteine 169 of Kallikrein-10

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 235 of Kallikrein-10

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-10 between cysteines 162 and 263 (129 and 232 respectively in this structure).

Details

Redox score ?
82
PDB code
5lpf
Structure name
kallikrein-related peptidase 10
Structure deposition date
2016-08-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43240
Residue number A
162
Residue number B
263
Peptide name
Kallikrein-10

Ligandability

Cysteine 162 of Kallikrein-10

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 263 of Kallikrein-10

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-10 between cysteines 71 and 87 (42 and 58 respectively in this structure).

Details

Redox score ?
81
PDB code
5lpe
Structure name
kallikrein-related peptidase 10 complex with zn2+
Structure deposition date
2016-08-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43240
Residue number A
71
Residue number B
87
Peptide name
Kallikrein-10

Ligandability

Cysteine 71 of Kallikrein-10

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 87 of Kallikrein-10

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-10 between cysteines 201 and 215 (168 and 182 respectively in this structure).

Details

Redox score ?
81
PDB code
5lpe
Structure name
kallikrein-related peptidase 10 complex with zn2+
Structure deposition date
2016-08-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43240
Residue number A
201
Residue number B
215
Peptide name
Kallikrein-10

Ligandability

Cysteine 201 of Kallikrein-10

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 215 of Kallikrein-10

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-10 between cysteines 225 and 250 (191 and 220 respectively in this structure).

Details

Redox score ?
80
PDB code
5lpf
Structure name
kallikrein-related peptidase 10
Structure deposition date
2016-08-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43240
Residue number A
225
Residue number B
250
Peptide name
Kallikrein-10

Ligandability

Cysteine 225 of Kallikrein-10

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 250 of Kallikrein-10

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-10 between cysteines 235 and 263 (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 ?
38
PDB code
5lpe
Structure name
kallikrein-related peptidase 10 complex with zn2+
Structure deposition date
2016-08-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43240
Residue number A
235
Residue number B
263
Peptide name
Kallikrein-10

Ligandability

Cysteine 235 of Kallikrein-10

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 263 of Kallikrein-10

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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