ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Insulin-like peptide INSL5

Intermolecular
Cysteine 47 of Relaxin-3 and cysteine 135
Cysteine 35 of Relaxin-3 and cysteine 122
Cysteine 35 of Relaxin-3 and cysteine 121
Cysteine 35 of Relaxin-3 and cysteine 126
Intramolecular
Cysteine 121 and cysteine 126
Cysteine 121 and cysteine 122
Cysteine 122 and cysteine 126
A redox-regulated disulphide may form between cysteine 47 of Relaxin-3 and cysteine 135 of Insulin-like peptide INSL5 (22 and 24 respectively in this structure).

Details

Redox score ?
91
PDB code
2k1v
Structure name
r3/i5 relaxin chimera
Structure deposition date
2008-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide A name
Relaxin-3
Peptide B name
Insulin-like peptide INSL5
Peptide A accession
Q8WXF3
Peptide B accession
Q9Y5Q6
Peptide A residue number
47
Peptide B residue number
135

Ligandability

Cysteine 47 of Relaxin-3

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 135 of Insulin-like peptide INSL5

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 between cysteine 35 of Relaxin-3 and cysteine 122 of Insulin-like peptide INSL5 (10 and 11 respectively in this structure).

Details

Redox score ?
85
PDB code
2k1v
Structure name
r3/i5 relaxin chimera
Structure deposition date
2008-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide A name
Relaxin-3
Peptide B name
Insulin-like peptide INSL5
Peptide A accession
Q8WXF3
Peptide B accession
Q9Y5Q6
Peptide A residue number
35
Peptide B residue number
122

Ligandability

Cysteine 35 of Relaxin-3

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 122 of Insulin-like peptide INSL5

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 between cysteine 35 of Relaxin-3 and cysteine 121 of Insulin-like peptide INSL5 (10 and 10 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
2k1v
Structure name
r3/i5 relaxin chimera
Structure deposition date
2008-03-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide A name
Relaxin-3
Peptide B name
Insulin-like peptide INSL5
Peptide A accession
Q8WXF3
Peptide B accession
Q9Y5Q6
Peptide A residue number
35
Peptide B residue number
121

Ligandability

Cysteine 35 of Relaxin-3

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 121 of Insulin-like peptide INSL5

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 between cysteine 35 of Relaxin-3 and cysteine 126 of Insulin-like peptide INSL5 (10 and 15 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
2k1v
Structure name
r3/i5 relaxin chimera
Structure deposition date
2008-03-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide A name
Relaxin-3
Peptide B name
Insulin-like peptide INSL5
Peptide A accession
Q8WXF3
Peptide B accession
Q9Y5Q6
Peptide A residue number
35
Peptide B residue number
126

Ligandability

Cysteine 35 of Relaxin-3

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 126 of Insulin-like peptide INSL5

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 Insulin-like peptide INSL5 between cysteines 121 and 126 (10 and 15 respectively in this structure).

Details

Redox score ?
87
PDB code
2k1v
Structure name
r3/i5 relaxin chimera
Structure deposition date
2008-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y5Q6
Residue number A
121
Residue number B
126
Peptide name
Insulin-like peptide INSL5

Ligandability

Cysteine 121 of Insulin-like peptide INSL5

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 126 of Insulin-like peptide INSL5

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 Insulin-like peptide INSL5 between cysteines 121 and 122 (10 and 11 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
2k1v
Structure name
r3/i5 relaxin chimera
Structure deposition date
2008-03-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y5Q6
Residue number A
121
Residue number B
122
Peptide name
Insulin-like peptide INSL5

Ligandability

Cysteine 121 of Insulin-like peptide INSL5

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 122 of Insulin-like peptide INSL5

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 Insulin-like peptide INSL5 between cysteines 122 and 126 (11 and 15 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
2k1v
Structure name
r3/i5 relaxin chimera
Structure deposition date
2008-03-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y5Q6
Residue number A
122
Residue number B
126
Peptide name
Insulin-like peptide INSL5

Ligandability

Cysteine 122 of Insulin-like peptide INSL5

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 126 of Insulin-like peptide INSL5

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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