Epithelial splicing regulatory protein 1
Intramolecular
Cysteine 146 and cysteine 147
Cysteine 446 and cysteine 523
Cysteine 350 and cysteine 379
Cysteine 105 and cysteine 132
Cysteine 105 and cysteine 107
7wrn A 146 A 147
A redox-regulated disulphide may form within Epithelial splicing regulatory protein 1 between cysteines 146 and 147.
Details
Redox score ?
73
PDB code
7wrn
Structure name
esrp1 rnaseh-qrrm1 tandem domain
Structure deposition date
2022-01-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
11
% buried
39
Peptide accession
Q6NXG1
Residue number A
146
Residue number B
147
Peptide name
Epithelial splicing regulatory protein 1
Ligandability
Cysteine 146 of Epithelial splicing regulatory protein 1
Cysteine 147 of Epithelial splicing regulatory protein 1
7vkj C 446 C 523
A redox-regulated disulphide may form within Epithelial splicing regulatory protein 1 between cysteines 446 and 523. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
7vkj
Structure name
structure of esrp1 qrrm3 domain
Structure deposition date
2021-09-30
Thiol separation (Å)
5
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
78
Peptide accession
Q6NXG1
Residue number A
446
Residue number B
523
Peptide name
Epithelial splicing regulatory protein 1
Ligandability
Cysteine 446 of Epithelial splicing regulatory protein 1
Cysteine 523 of Epithelial splicing regulatory protein 1
2dha A 190 A 219
A redox-regulated disulphide may form within Epithelial splicing regulatory protein 1 between cysteines 350 and 379 (190 and 219 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
2dha
Structure name
solution structure of the second rna recognition motif in hypothetical protein flj201171
Structure deposition date
2006-03-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
52
Minimum pKa ?
9
% buried
12
Peptide accession
Q9NXL8
Residue number A
350
Residue number B
379
Peptide name
Epithelial splicing regulatory protein 1
Ligandability
Cysteine 350 of Epithelial splicing regulatory protein 1
Cysteine 379 of Epithelial splicing regulatory protein 1
7wrn A 105 A 132
A redox-regulated disulphide may form within Epithelial splicing regulatory protein 1 between cysteines 105 and 132. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
7wrn
Structure name
esrp1 rnaseh-qrrm1 tandem domain
Structure deposition date
2022-01-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
88
Peptide accession
Q6NXG1
Residue number A
105
Residue number B
132
Peptide name
Epithelial splicing regulatory protein 1
Ligandability
Cysteine 105 of Epithelial splicing regulatory protein 1
Cysteine 132 of Epithelial splicing regulatory protein 1
7wrn A 105 A 107
A redox-regulated disulphide may form within Epithelial splicing regulatory protein 1 between cysteines 105 and 107. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
7wrn
Structure name
esrp1 rnaseh-qrrm1 tandem domain
Structure deposition date
2022-01-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
85
Minimum pKa ?
11
% buried
90
Peptide accession
Q6NXG1
Residue number A
105
Residue number B
107
Peptide name
Epithelial splicing regulatory protein 1
Ligandability
Cysteine 105 of Epithelial splicing regulatory protein 1
Cysteine 107 of Epithelial splicing regulatory protein 1
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