ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Peptidyl-prolyl cis-trans isomerase FKBP5

Intermolecular
Cysteine 183 and cysteine 183
Intramolecular
Cysteine 339 and cysteine 340
Cysteine 326 and cysteine 339
Cysteine 103 and cysteine 107
A redox-regulated disulphide may form between two units of Peptidyl-prolyl cis-trans isomerase FKBP5 at cysteines 183 and 183. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
3o5d
Structure name
crystal structure of a fragment of fkbp51 comprising the fk1 and fk2 domains
Structure deposition date
2010-07-28
Thiol separation (Å)
5
Half-sphere exposure sum ?
66
Minimum pKa ?
14
% buried
84
Peptide A name
Peptidyl-prolyl cis-trans isomerase FKBP5
Peptide B name
Peptidyl-prolyl cis-trans isomerase FKBP5
Peptide A accession
Q13451
Peptide B accession
Q13451
Peptide A residue number
183
Peptide B residue number
183

Ligandability

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 Peptidyl-prolyl cis-trans isomerase FKBP5 between cysteines 339 and 340. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
1kt1
Structure name
structure of the large fkbp-like protein, fkbp51, involved in steroid receptor complexes
Structure deposition date
2002-01-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
73
Peptide accession
Q9XSH5
Residue number A
339
Residue number B
340
Peptide name
Peptidyl-prolyl cis-trans isomerase FKBP5

Ligandability

Cysteine 339 of Peptidyl-prolyl cis-trans isomerase FKBP5

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 340 of Peptidyl-prolyl cis-trans isomerase FKBP5

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 Peptidyl-prolyl cis-trans isomerase FKBP5 between cysteines 326 and 339. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
1kt1
Structure name
structure of the large fkbp-like protein, fkbp51, involved in steroid receptor complexes
Structure deposition date
2002-01-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
68
Peptide accession
Q9XSH5
Residue number A
326
Residue number B
339
Peptide name
Peptidyl-prolyl cis-trans isomerase FKBP5

Ligandability

Cysteine 326 of Peptidyl-prolyl cis-trans isomerase FKBP5

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 339 of Peptidyl-prolyl cis-trans isomerase FKBP5

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 Peptidyl-prolyl cis-trans isomerase FKBP5 between cysteines 103 and 107. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
4w9p
Structure name
the fk1 domain of fkbp51 in complex with (1s,5s,6r)-10-[(3,5- dichlorophenyl)sulfonyl]-5-[(1s)-1,2-dihydroxyethyl]-3-[2-(3,4- dimethoxyphenoxy)ethyl]-3,10-diazabicyclo[4
Structure deposition date
2014-08-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
92
Peptide accession
Q13451
Residue number A
103
Residue number B
107
Peptide name
Peptidyl-prolyl cis-trans isomerase FKBP5

Ligandability

Cysteine 103 of Peptidyl-prolyl cis-trans isomerase FKBP5

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 107 of Peptidyl-prolyl cis-trans isomerase FKBP5

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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