Peptidyl-prolyl cis-trans isomerase D
1ihg A 52 A 181
A redox-regulated disulphide may form within Peptidyl-prolyl cis-trans isomerase D between cysteines 52 and 181. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
1ihg
Structure name
bovine cyclophilin 40, monoclinic form
Structure deposition date
2001-04-19
Thiol separation (Å)
5
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
86
Peptide accession
P26882
Residue number A
52
Residue number B
181
Peptide name
Peptidyl-prolyl cis-trans isomerase D
Ligandability
Cysteine 52 of Peptidyl-prolyl cis-trans isomerase D
Cysteine 181 of Peptidyl-prolyl cis-trans isomerase D
1iip A 71 A 181
A redox-regulated disulphide may form within Peptidyl-prolyl cis-trans isomerase D between cysteines 71 and 181. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
1iip
Structure name
bovine cyclophilin 40, tetragonal form
Structure deposition date
2001-04-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
82
Peptide accession
P26882
Residue number A
71
Residue number B
181
Peptide name
Peptidyl-prolyl cis-trans isomerase D
Ligandability
Cysteine 71 of Peptidyl-prolyl cis-trans isomerase D
Cysteine 181 of Peptidyl-prolyl cis-trans isomerase D
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