ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Cathepsin K

Intramolecular
Cysteine 269 and cysteine 318
Cysteine 136 and cysteine 177
Cysteine 170 and cysteine 210
Cysteine 136 and cysteine 139
Cysteine 139 and cysteine 177
A redox-regulated disulphide may form within Cathepsin K between cysteines 269 and 318 (155 and 204 respectively in this structure).

Details

Redox score ?
85
PDB code
2ftd
Structure name
crystal structure of cathepsin k complexed with 7-methyl- substituted azepan-3-one compound
Structure deposition date
2006-01-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P61277
Residue number A
269
Residue number B
318
Peptide name
Cathepsin K

Ligandability

Cysteine 269 of Cathepsin K

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 318 of Cathepsin K

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 Cathepsin K between cysteines 136 and 177 (22 and 63 respectively in this structure).

Details

Redox score ?
85
PDB code
2f7d
Structure name
a mutant rabbit cathepsin k with a nitrile inhibitor
Structure deposition date
2005-11-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43236
Residue number A
136
Residue number B
177
Peptide name
Cathepsin K

Ligandability

Cysteine 136 of Cathepsin K

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 177 of Cathepsin K

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 Cathepsin K between cysteines 170 and 210 (56 and 96 respectively in this structure).

Details

Redox score ?
84
PDB code
1q6k
Structure name
cathepsin k complexed with t-butyl(1s)-1-cyclohexyl-2- oxoethylcarbamate
Structure deposition date
2003-08-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43235
Residue number A
170
Residue number B
210
Peptide name
Cathepsin K

Ligandability

Cysteine 170 of Cathepsin K

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 210 of Cathepsin K

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 Cathepsin K between cysteines 136 and 139 (22 and 25 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
2aux
Structure name
cathepsin k complexed with a semicarbazone inhibitor
Structure deposition date
2005-08-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
13
% buried
nan
Peptide accession
P43235
Residue number A
136
Residue number B
139
Peptide name
Cathepsin K

Ligandability

Cysteine 136 of Cathepsin K

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 139 of Cathepsin K

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 Cathepsin K between cysteines 139 and 177 (25 and 63 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
4n8w
Structure name
cathepsin k - chondroitin sulfate complex
Structure deposition date
2013-10-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
10
% buried
nan
Peptide accession
P43235
Residue number A
139
Residue number B
177
Peptide name
Cathepsin K

Ligandability

Cysteine 139 of Cathepsin K

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 177 of Cathepsin K

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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