ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Peptidyl-prolyl cis-trans isomerase G

Intramolecular
Cysteine 10 and cysteine 44
Cysteine 33 and cysteine 37 L
Cysteine 44 and cysteine 174
Cysteine 63 and cysteine 174
Cysteine 10 and cysteine 174
Cysteine 10 and cysteine 37
Cysteine 10 and cysteine 42
Cysteine 42 and cysteine 44
A redox-regulated disulphide may form within Peptidyl-prolyl cis-trans isomerase G between cysteines 10 and 44.

Details

Redox score ?
69
PDB code
2gw2
Structure name
crystal structure of the peptidyl-prolyl isomerase domain of human cyclophilin g
Structure deposition date
2006-05-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q13427
Residue number A
10
Residue number B
44
Peptide name
Peptidyl-prolyl cis-trans isomerase G

Ligandability

Cysteine 10 of Peptidyl-prolyl cis-trans isomerase G

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 44 of Peptidyl-prolyl cis-trans isomerase G

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 G between cysteines 33 and 37.

Details

Redox score ?
61
PDB code
2wfj
Structure name
atomic resolution crystal structure of the ppiase domain of human cyclophilin g in complex with cyclosporin a
Structure deposition date
2009-04-06
Thiol separation (Å)
6
Half-sphere exposure sum ?
72
Minimum pKa ?
10
% buried
70
Peptide accession
Q13427
Residue number A
33
Residue number B
37
Peptide name
Peptidyl-prolyl cis-trans isomerase G

Ligandability

Cysteine 33 of Peptidyl-prolyl cis-trans isomerase G

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 37 of Peptidyl-prolyl cis-trans isomerase G

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 G between cysteines 44 and 174. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
2wfi
Structure name
atomic resolution crystal structure of the ppiase domain of human cyclophilin g
Structure deposition date
2009-04-06
Thiol separation (Å)
5
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
82
Peptide accession
Q13427
Residue number A
44
Residue number B
174
Peptide name
Peptidyl-prolyl cis-trans isomerase G

Ligandability

Cysteine 44 of Peptidyl-prolyl cis-trans isomerase G

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 174 of Peptidyl-prolyl cis-trans isomerase G

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 G between cysteines 63 and 174. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
2gw2
Structure name
crystal structure of the peptidyl-prolyl isomerase domain of human cyclophilin g
Structure deposition date
2006-05-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q13427
Residue number A
63
Residue number B
174
Peptide name
Peptidyl-prolyl cis-trans isomerase G

Ligandability

Cysteine 63 of Peptidyl-prolyl cis-trans isomerase G

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 174 of Peptidyl-prolyl cis-trans isomerase G

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 G between cysteines 10 and 174. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
2gw2
Structure name
crystal structure of the peptidyl-prolyl isomerase domain of human cyclophilin g
Structure deposition date
2006-05-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q13427
Residue number A
10
Residue number B
174
Peptide name
Peptidyl-prolyl cis-trans isomerase G

Ligandability

Cysteine 10 of Peptidyl-prolyl cis-trans isomerase G

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 174 of Peptidyl-prolyl cis-trans isomerase G

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 G between cysteines 10 and 37. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
2gw2
Structure name
crystal structure of the peptidyl-prolyl isomerase domain of human cyclophilin g
Structure deposition date
2006-05-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q13427
Residue number A
10
Residue number B
37
Peptide name
Peptidyl-prolyl cis-trans isomerase G

Ligandability

Cysteine 10 of Peptidyl-prolyl cis-trans isomerase G

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 37 of Peptidyl-prolyl cis-trans isomerase G

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 G between cysteines 10 and 42. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
2gw2
Structure name
crystal structure of the peptidyl-prolyl isomerase domain of human cyclophilin g
Structure deposition date
2006-05-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q13427
Residue number A
10
Residue number B
42
Peptide name
Peptidyl-prolyl cis-trans isomerase G

Ligandability

Cysteine 10 of Peptidyl-prolyl cis-trans isomerase G

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 42 of Peptidyl-prolyl cis-trans isomerase G

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 G between cysteines 42 and 44. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
2gw2
Structure name
crystal structure of the peptidyl-prolyl isomerase domain of human cyclophilin g
Structure deposition date
2006-05-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q13427
Residue number A
42
Residue number B
44
Peptide name
Peptidyl-prolyl cis-trans isomerase G

Ligandability

Cysteine 42 of Peptidyl-prolyl cis-trans isomerase G

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 44 of Peptidyl-prolyl cis-trans isomerase G

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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