ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Peptidyl-prolyl cis-trans isomerase A

Intramolecular
Cysteine 52 and cysteine 161 L
Cysteine 52 and cysteine 62 L
Cysteine 62 and cysteine 115 L
A redox-regulated disulphide may form within Peptidyl-prolyl cis-trans isomerase A between cysteines 52 and 161. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
2n0t
Structure name
structural ensemble of the enzyme cyclophilin reveals an orchestrated mode of action at atomic resolution
Structure deposition date
2015-03-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
28
Peptide accession
P62937
Residue number A
52
Residue number B
161
Peptide name
Peptidyl-prolyl cis-trans isomerase A

Ligandability

Cysteine 52 of Peptidyl-prolyl cis-trans isomerase A

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 161 of Peptidyl-prolyl cis-trans isomerase A

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Peptidyl-prolyl cis-trans isomerase A between cysteines 52 and 62. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
1oca
Structure name
human cyclophilin a, unligated, nmr, 20 structures
Structure deposition date
1997-07-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
92
Minimum pKa ?
10
% buried
73
Peptide accession
P62937
Residue number A
52
Residue number B
62
Peptide name
Peptidyl-prolyl cis-trans isomerase A

Ligandability

Cysteine 52 of Peptidyl-prolyl cis-trans isomerase A

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 62 of Peptidyl-prolyl cis-trans isomerase A

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Peptidyl-prolyl cis-trans isomerase A between cysteines 62 and 115. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
5hsv
Structure name
x-ray structure of a cypa-alisporivir complex at 1
Structure deposition date
2016-01-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
93
Peptide accession
P62938
Residue number A
62
Residue number B
115
Peptide name
Peptidyl-prolyl cis-trans isomerase A

Ligandability

Cysteine 62 of Peptidyl-prolyl cis-trans isomerase A

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 115 of Peptidyl-prolyl cis-trans isomerase A

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.

Ligandable in the dataset of Kuljanin et al.

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