Peptidyl-prolyl cis-trans isomerase H
1qoi A 47 A 174
A redox-regulated disulphide may form within Peptidyl-prolyl cis-trans isomerase H between cysteines 47 and 174.
Details
Redox score ?
62
PDB code
1qoi
Structure name
u4/u6 snrnp-specific cyclophilin snucyp-20
Structure deposition date
1999-11-09
Thiol separation (Å)
5
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
84
Peptide accession
O43447
Residue number A
47
Residue number B
174
Peptide name
Peptidyl-prolyl cis-trans isomerase H
Ligandability
Cysteine 47 of Peptidyl-prolyl cis-trans isomerase H
Cysteine 174 of Peptidyl-prolyl cis-trans isomerase H
1qoi A 128 A 131
A redox-regulated disulphide may form within Peptidyl-prolyl cis-trans isomerase H between cysteines 128 and 131. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
1qoi
Structure name
u4/u6 snrnp-specific cyclophilin snucyp-20
Structure deposition date
1999-11-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
11
% buried
50
Peptide accession
O43447
Residue number A
128
Residue number B
131
Peptide name
Peptidyl-prolyl cis-trans isomerase H
Ligandability
Cysteine 128 of Peptidyl-prolyl cis-trans isomerase H
Cysteine 131 of Peptidyl-prolyl cis-trans isomerase H
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