ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Insulin-like growth factor 2 receptor variant

Intermolecular
Cysteine 1521 and cysteine 75 of Insulin-like growth factor II
Intramolecular
Cysteine 1482 and cysteine 1489
Cysteine 1521 and cysteine 1557
Cysteine 1439 and cysteine 1476
Cysteine 1537 and cysteine 1569
A redox-regulated disulphide may form between cysteine 1521 of Insulin-like growth factor 2 receptor variant and cysteine 75 of Insulin-like growth factor II (1598 and 51 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
2l29
Structure name
complex structure of e4 mutant human igf2r domain 11 bound to igf-ii
Structure deposition date
2010-08-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin-like growth factor 2 receptor variant
Peptide B name
Insulin-like growth factor II
Peptide A accession
Q59EZ3
Peptide B accession
P01344
Peptide A residue number
1521
Peptide B residue number
75

Ligandability

Cysteine 1521 of Insulin-like growth factor 2 receptor variant

Cysteine 75 of Insulin-like growth factor II

A redox-regulated disulphide may form within Insulin-like growth factor 2 receptor variant between cysteines 1482 and 1489 (1559 and 1566 respectively in this structure).

Details

Redox score ?
83
PDB code
2l29
Structure name
complex structure of e4 mutant human igf2r domain 11 bound to igf-ii
Structure deposition date
2010-08-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q59EZ3
Residue number A
1482
Residue number B
1489
Peptide name
Insulin-like growth factor 2 receptor variant

Ligandability

Cysteine 1482 of Insulin-like growth factor 2 receptor variant

Cysteine 1489 of Insulin-like growth factor 2 receptor variant

A redox-regulated disulphide may form within Insulin-like growth factor 2 receptor variant between cysteines 1521 and 1557 (1598 and 1634 respectively in this structure).

Details

Redox score ?
83
PDB code
2l29
Structure name
complex structure of e4 mutant human igf2r domain 11 bound to igf-ii
Structure deposition date
2010-08-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q59EZ3
Residue number A
1521
Residue number B
1557
Peptide name
Insulin-like growth factor 2 receptor variant

Ligandability

Cysteine 1521 of Insulin-like growth factor 2 receptor variant

Cysteine 1557 of Insulin-like growth factor 2 receptor variant

A redox-regulated disulphide may form within Insulin-like growth factor 2 receptor variant between cysteines 1439 and 1476 (1516 and 1553 respectively in this structure).

Details

Redox score ?
83
PDB code
2l29
Structure name
complex structure of e4 mutant human igf2r domain 11 bound to igf-ii
Structure deposition date
2010-08-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q59EZ3
Residue number A
1439
Residue number B
1476
Peptide name
Insulin-like growth factor 2 receptor variant

Ligandability

Cysteine 1439 of Insulin-like growth factor 2 receptor variant

Cysteine 1476 of Insulin-like growth factor 2 receptor variant

A redox-regulated disulphide may form within Insulin-like growth factor 2 receptor variant between cysteines 1537 and 1569 (1614 and 1646 respectively in this structure).

Details

Redox score ?
81
PDB code
2m68
Structure name
nmr solution structure ensemble of 3-4d mutant domain 11 igf2r in complex with igf2 (domain 11 structure only)
Structure deposition date
2013-03-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q59EZ3
Residue number A
1537
Residue number B
1569
Peptide name
Insulin-like growth factor 2 receptor variant

Ligandability

Cysteine 1537 of Insulin-like growth factor 2 receptor variant

Cysteine 1569 of Insulin-like growth factor 2 receptor variant

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