ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Peptidyl-prolyl cis-trans isomerase F, mitochondrial

Intramolecular
Cysteine 82 and cysteine 203
Cysteine 104 and cysteine 157
A redox-regulated disulphide may form within Peptidyl-prolyl cis-trans isomerase F, mitochondrial between cysteines 82 and 203.

Details

Redox score ?
63
PDB code
4j5b
Structure name
human cyclophilin d complexed with an inhibitor
Structure deposition date
2013-02-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
81
Peptide accession
P30405
Residue number A
82
Residue number B
203
Peptide name
Peptidyl-prolyl cis-trans isomerase F, mitochondrial

Ligandability

Cysteine 82 of Peptidyl-prolyl cis-trans isomerase F, mitochondrial

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 203 of Peptidyl-prolyl cis-trans isomerase F, mitochondrial

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 F, mitochondrial between cysteines 104 and 157. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
3r4g
Structure name
human cyclophilin d complexed with a fragment
Structure deposition date
2011-03-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
11
% buried
90
Peptide accession
P30405
Residue number A
104
Residue number B
157
Peptide name
Peptidyl-prolyl cis-trans isomerase F, mitochondrial

Ligandability

Cysteine 104 of Peptidyl-prolyl cis-trans isomerase F, mitochondrial

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 157 of Peptidyl-prolyl cis-trans isomerase F, mitochondrial

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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